Serveur d'exploration MERS

Attention, ce site est en cours de développement !
Attention, site généré par des moyens informatiques à partir de corpus bruts.
Les informations ne sont donc pas validées.

Structural and conformational analysis of scorpion (Buthus sindicus) hemocyanin using low resolution techniques.

Identifieur interne : 002B31 ( Main/Exploration ); précédent : 002B30; suivant : 002B32

Structural and conformational analysis of scorpion (Buthus sindicus) hemocyanin using low resolution techniques.

Auteurs : Syed Abid Ali [Pakistan] ; J Günter Grossmann ; Atiya Abbasi ; Wolfgang Voelter

Source :

RBID : pubmed:17584175

Descripteurs français

English descriptors

Abstract

Blue oxygen binding protein hemocyanin from scorpion Buthus sindicus has been investigated using low resolution techniques. The native protein is a polymer of eight different types of subunits arranged in four cubic hexameric form (4x6-mers) as previously annotated using a combination of various types of chromatographic and electrophoretic techniques. In addition, both "top face" as well as the "side view" of the native assembly has also been identified from the negatively stained specimens using transmission electron microscopy confirming the overall structural features of arthropodan hemocyanins. These results are also supported from data obtained from another low resolution technique i.e. Small Angle X-ray scattering (SAXS). SAXS results under oxygenated and deoxygenated states represent a validation case for this technique with key conformational changes of Rg 88.0 --> 86.0 A; +/- 1% (Dmax 280.0 --> 290.0 A; +/- 2%), respectively suggesting that the oxygenated hemocyanin is longer then the deoxygenated hemocyanin by almost 2 A;. Likewise, active conformations of the purified structural and functional subunit Bsin1 under oxygenated and deoxygenated states also determined by SAXS measurements revealed a Rg value of 25.2 --> 25.7 A; +/- 1% (Dmax 75.0 --> 75.5 A; +/- 2%), respectively suggesting very little or no contribution of the individual subunit in the overall conformational change in the native assembly during molecular breathing. Preliminary molecular shapes for the oxy-molecules, calculated directly from the scattering profile-alone in a model-independent procedure, superimpose well on other closely related known three-dimensional structures of the same size. Structural and functional aspects of the native as well as purified subunit and the application of these low resolution techniques like transmission electron microscopy and Small Angle X-ray scattering have been discussed.

DOI: 10.2174/092986607780782731
PubMed: 17584175


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

<record>
<TEI>
<teiHeader>
<fileDesc>
<titleStmt>
<title xml:lang="en">Structural and conformational analysis of scorpion (Buthus sindicus) hemocyanin using low resolution techniques.</title>
<author>
<name sortKey="Ali, Syed Abid" sort="Ali, Syed Abid" uniqKey="Ali S" first="Syed Abid" last="Ali">Syed Abid Ali</name>
<affiliation wicri:level="1">
<nlm:affiliation>International Center for Chemical and Biological Sciences, HEJ Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan. syedabidali@cyber.net.pk</nlm:affiliation>
<country xml:lang="fr">Pakistan</country>
<wicri:regionArea>International Center for Chemical and Biological Sciences, HEJ Research Institute of Chemistry, University of Karachi, Karachi-75270</wicri:regionArea>
<wicri:noRegion>Karachi-75270</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Grossmann, J Gunter" sort="Grossmann, J Gunter" uniqKey="Grossmann J" first="J Günter" last="Grossmann">J Günter Grossmann</name>
</author>
<author>
<name sortKey="Abbasi, Atiya" sort="Abbasi, Atiya" uniqKey="Abbasi A" first="Atiya" last="Abbasi">Atiya Abbasi</name>
</author>
<author>
<name sortKey="Voelter, Wolfgang" sort="Voelter, Wolfgang" uniqKey="Voelter W" first="Wolfgang" last="Voelter">Wolfgang Voelter</name>
</author>
</titleStmt>
<publicationStmt>
<idno type="wicri:source">PubMed</idno>
<date when="2007">2007</date>
<idno type="RBID">pubmed:17584175</idno>
<idno type="pmid">17584175</idno>
<idno type="doi">10.2174/092986607780782731</idno>
<idno type="wicri:Area/PubMed/Corpus">002178</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002178</idno>
<idno type="wicri:Area/PubMed/Curation">002178</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002178</idno>
<idno type="wicri:Area/PubMed/Checkpoint">002033</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002033</idno>
<idno type="wicri:Area/Ncbi/Merge">000528</idno>
<idno type="wicri:Area/Ncbi/Curation">000528</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000528</idno>
<idno type="wicri:doubleKey">0929-8665:2007:Ali S:structural:and:conformational</idno>
<idno type="wicri:Area/Main/Merge">002B57</idno>
<idno type="wicri:Area/Main/Curation">002B31</idno>
<idno type="wicri:Area/Main/Exploration">002B31</idno>
</publicationStmt>
<sourceDesc>
<biblStruct>
<analytic>
<title xml:lang="en">Structural and conformational analysis of scorpion (Buthus sindicus) hemocyanin using low resolution techniques.</title>
<author>
<name sortKey="Ali, Syed Abid" sort="Ali, Syed Abid" uniqKey="Ali S" first="Syed Abid" last="Ali">Syed Abid Ali</name>
<affiliation wicri:level="1">
<nlm:affiliation>International Center for Chemical and Biological Sciences, HEJ Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan. syedabidali@cyber.net.pk</nlm:affiliation>
<country xml:lang="fr">Pakistan</country>
<wicri:regionArea>International Center for Chemical and Biological Sciences, HEJ Research Institute of Chemistry, University of Karachi, Karachi-75270</wicri:regionArea>
<wicri:noRegion>Karachi-75270</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Grossmann, J Gunter" sort="Grossmann, J Gunter" uniqKey="Grossmann J" first="J Günter" last="Grossmann">J Günter Grossmann</name>
</author>
<author>
<name sortKey="Abbasi, Atiya" sort="Abbasi, Atiya" uniqKey="Abbasi A" first="Atiya" last="Abbasi">Atiya Abbasi</name>
</author>
<author>
<name sortKey="Voelter, Wolfgang" sort="Voelter, Wolfgang" uniqKey="Voelter W" first="Wolfgang" last="Voelter">Wolfgang Voelter</name>
</author>
</analytic>
<series>
<title level="j">Protein and peptide letters</title>
<idno type="ISSN">0929-8665</idno>
<imprint>
<date when="2007" type="published">2007</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc>
<textClass>
<keywords scheme="KwdEn" xml:lang="en">
<term>Animals</term>
<term>Hemocyanins (chemistry)</term>
<term>Microscopy, Electron, Transmission</term>
<term>Models, Molecular</term>
<term>Oxygen (metabolism)</term>
<term>Protein Conformation</term>
<term>Protein Structure, Quaternary</term>
<term>Scattering, Small Angle</term>
<term>Scorpions (chemistry)</term>
<term>X-Ray Diffraction</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Animaux</term>
<term>Conformation des protéines</term>
<term>Diffraction des rayons X</term>
<term>Diffusion aux petits angles</term>
<term>Microscopie électronique à transmission</term>
<term>Modèles moléculaires</term>
<term>Oxygène (métabolisme)</term>
<term>Scorpions ()</term>
<term>Structure quaternaire des protéines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en">
<term>Hemocyanins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Oxygen</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en">
<term>Scorpions</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Oxygène</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Animals</term>
<term>Microscopy, Electron, Transmission</term>
<term>Models, Molecular</term>
<term>Protein Conformation</term>
<term>Protein Structure, Quaternary</term>
<term>Scattering, Small Angle</term>
<term>X-Ray Diffraction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Animaux</term>
<term>Conformation des protéines</term>
<term>Diffraction des rayons X</term>
<term>Diffusion aux petits angles</term>
<term>Microscopie électronique à transmission</term>
<term>Modèles moléculaires</term>
<term>Scorpions</term>
<term>Structure quaternaire des protéines</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">Blue oxygen binding protein hemocyanin from scorpion Buthus sindicus has been investigated using low resolution techniques. The native protein is a polymer of eight different types of subunits arranged in four cubic hexameric form (4x6-mers) as previously annotated using a combination of various types of chromatographic and electrophoretic techniques. In addition, both "top face" as well as the "side view" of the native assembly has also been identified from the negatively stained specimens using transmission electron microscopy confirming the overall structural features of arthropodan hemocyanins. These results are also supported from data obtained from another low resolution technique i.e. Small Angle X-ray scattering (SAXS). SAXS results under oxygenated and deoxygenated states represent a validation case for this technique with key conformational changes of Rg 88.0 --> 86.0 A; +/- 1% (Dmax 280.0 --> 290.0 A; +/- 2%), respectively suggesting that the oxygenated hemocyanin is longer then the deoxygenated hemocyanin by almost 2 A;. Likewise, active conformations of the purified structural and functional subunit Bsin1 under oxygenated and deoxygenated states also determined by SAXS measurements revealed a Rg value of 25.2 --> 25.7 A; +/- 1% (Dmax 75.0 --> 75.5 A; +/- 2%), respectively suggesting very little or no contribution of the individual subunit in the overall conformational change in the native assembly during molecular breathing. Preliminary molecular shapes for the oxy-molecules, calculated directly from the scattering profile-alone in a model-independent procedure, superimpose well on other closely related known three-dimensional structures of the same size. Structural and functional aspects of the native as well as purified subunit and the application of these low resolution techniques like transmission electron microscopy and Small Angle X-ray scattering have been discussed.</div>
</front>
</TEI>
<affiliations>
<list>
<country>
<li>Pakistan</li>
</country>
</list>
<tree>
<noCountry>
<name sortKey="Abbasi, Atiya" sort="Abbasi, Atiya" uniqKey="Abbasi A" first="Atiya" last="Abbasi">Atiya Abbasi</name>
<name sortKey="Grossmann, J Gunter" sort="Grossmann, J Gunter" uniqKey="Grossmann J" first="J Günter" last="Grossmann">J Günter Grossmann</name>
<name sortKey="Voelter, Wolfgang" sort="Voelter, Wolfgang" uniqKey="Voelter W" first="Wolfgang" last="Voelter">Wolfgang Voelter</name>
</noCountry>
<country name="Pakistan">
<noRegion>
<name sortKey="Ali, Syed Abid" sort="Ali, Syed Abid" uniqKey="Ali S" first="Syed Abid" last="Ali">Syed Abid Ali</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002B31 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002B31 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    MersV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:17584175
   |texte=   Structural and conformational analysis of scorpion (Buthus sindicus) hemocyanin using low resolution techniques.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:17584175" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a MersV1 

Wicri

This area was generated with Dilib version V0.6.33.
Data generation: Mon Apr 20 23:26:43 2020. Site generation: Sat Mar 27 09:06:09 2021