All hierarchical levels are involved in conformational transitions of the 4 x 6-meric tarantula hemocyanin upon oxygenation.
Identifieur interne : 003346 ( Main/Exploration ); précédent : 003345; suivant : 003347All hierarchical levels are involved in conformational transitions of the 4 x 6-meric tarantula hemocyanin upon oxygenation.
Auteurs : Hermann Hartmann [Allemagne] ; Heinz DeckerSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2002.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Hemocyanins.
- chemical , isolation & purification : Hemocyanins.
- chemical , metabolism : Hemocyanins, Oxygen.
- Animals, Macromolecular Substances, Models, Molecular, Oxidation-Reduction, Protein Binding, Protein Conformation, Spiders.
Abstract
The respiratory protein of the tarantula Eurypelma californicum is a 4 x 6-meric hemocyanin that binds oxygen with high cooperativity. This requires the existence of different conformations which have been confirmed by small angle X-ray scattering (SAXS). Here we present reconstructed 3D-models of the oxy- and deoxy-forms of tarantula hemocyanins, as obtained by fitting small angle X-rays scattering curves on the basis of known X-ray structures and electron microscopy of related hemocyanins. For the first time, the involvement of movements at all levels of the quaternary structure was confirmed for an arthropod hemocyanin upon oxygenation. The two identical 2 x 6-meric half-molecules of the native 4 x 6-mer were shifted in the oxy-state along each other compared with the deoxy-state by about 14 A. In addition, the angle between the two 2 x 6-meric half-molecules increased by 13 degrees. Within these 2 x 6-mers the two hexamers were rotated against each other by about 26 degrees with respect to the deoxy-state. In addition, the distance between the two trimers of each hexamer increased upon oxygenation by about 2.5 A. These strongly coupled movements are based on the particular hierarchical structure of the 4 x 6-mer. It also shows a concept of allosteric interaction in hierarchically assembled proteins to guarantee the involvement of all subunits of a native oligomer to establish very high Hill coefficients.
DOI: 10.1016/s1570-9639(02)00459-4
PubMed: 12445474
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002481
- to stream PubMed, to step Curation: 002481
- to stream PubMed, to step Checkpoint: 002385
- to stream Ncbi, to step Merge: 000165
- to stream Ncbi, to step Curation: 000165
- to stream Ncbi, to step Checkpoint: 000165
- to stream Main, to step Merge: 003382
- to stream Main, to step Curation: 003346
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">All hierarchical levels are involved in conformational transitions of the 4 x 6-meric tarantula hemocyanin upon oxygenation.</title><author><name sortKey="Hartmann, Hermann" sort="Hartmann, Hermann" uniqKey="Hartmann H" first="Hermann" last="Hartmann">Hermann Hartmann</name><affiliation wicri:level="1"><nlm:affiliation>Institut für Molekulare Biophysik, Universität Mainz, Jakob Welder Weg 26, D-55099 Mainz, Germany. hartmann@biophysik.uni-mainz.de</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Molekulare Biophysik, Universität Mainz, Jakob Welder Weg 26, D-55099 Mainz</wicri:regionArea><wicri:noRegion>55099 Mainz</wicri:noRegion><wicri:noRegion>55099 Mainz</wicri:noRegion><wicri:noRegion>D-55099 Mainz</wicri:noRegion></affiliation></author><author><name sortKey="Decker, Heinz" sort="Decker, Heinz" uniqKey="Decker H" first="Heinz" last="Decker">Heinz Decker</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:12445474</idno><idno type="pmid">12445474</idno><idno type="doi">10.1016/s1570-9639(02)00459-4</idno><idno type="wicri:Area/PubMed/Corpus">002481</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002481</idno><idno type="wicri:Area/PubMed/Curation">002481</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002481</idno><idno type="wicri:Area/PubMed/Checkpoint">002385</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002385</idno><idno type="wicri:Area/Ncbi/Merge">000165</idno><idno type="wicri:Area/Ncbi/Curation">000165</idno><idno type="wicri:Area/Ncbi/Checkpoint">000165</idno><idno type="wicri:doubleKey">0006-3002:2002:Hartmann H:all:hierarchical:levels</idno><idno type="wicri:Area/Main/Merge">003382</idno><idno type="wicri:Area/Main/Curation">003346</idno><idno type="wicri:Area/Main/Exploration">003346</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">All hierarchical levels are involved in conformational transitions of the 4 x 6-meric tarantula hemocyanin upon oxygenation.</title><author><name sortKey="Hartmann, Hermann" sort="Hartmann, Hermann" uniqKey="Hartmann H" first="Hermann" last="Hartmann">Hermann Hartmann</name><affiliation wicri:level="1"><nlm:affiliation>Institut für Molekulare Biophysik, Universität Mainz, Jakob Welder Weg 26, D-55099 Mainz, Germany. hartmann@biophysik.uni-mainz.de</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Molekulare Biophysik, Universität Mainz, Jakob Welder Weg 26, D-55099 Mainz</wicri:regionArea><wicri:noRegion>55099 Mainz</wicri:noRegion><wicri:noRegion>55099 Mainz</wicri:noRegion><wicri:noRegion>D-55099 Mainz</wicri:noRegion></affiliation></author><author><name sortKey="Decker, Heinz" sort="Decker, Heinz" uniqKey="Decker H" first="Heinz" last="Decker">Heinz Decker</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Hemocyanins (chemistry)</term><term>Hemocyanins (isolation & purification)</term><term>Hemocyanins (metabolism)</term><term>Macromolecular Substances</term><term>Models, Molecular</term><term>Oxidation-Reduction</term><term>Oxygen (metabolism)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Spiders</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Araignées</term><term>Conformation des protéines</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Oxygène (métabolisme)</term><term>Structures macromoléculaires</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemocyanins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Hemocyanins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemocyanins</term><term>Oxygen</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxygène</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Macromolecular Substances</term><term>Models, Molecular</term><term>Oxidation-Reduction</term><term>Protein Binding</term><term>Protein Conformation</term><term>Spiders</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Araignées</term><term>Conformation des protéines</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Structures macromoléculaires</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The respiratory protein of the tarantula Eurypelma californicum is a 4 x 6-meric hemocyanin that binds oxygen with high cooperativity. This requires the existence of different conformations which have been confirmed by small angle X-ray scattering (SAXS). Here we present reconstructed 3D-models of the oxy- and deoxy-forms of tarantula hemocyanins, as obtained by fitting small angle X-rays scattering curves on the basis of known X-ray structures and electron microscopy of related hemocyanins. For the first time, the involvement of movements at all levels of the quaternary structure was confirmed for an arthropod hemocyanin upon oxygenation. The two identical 2 x 6-meric half-molecules of the native 4 x 6-mer were shifted in the oxy-state along each other compared with the deoxy-state by about 14 A. In addition, the angle between the two 2 x 6-meric half-molecules increased by 13 degrees. Within these 2 x 6-mers the two hexamers were rotated against each other by about 26 degrees with respect to the deoxy-state. In addition, the distance between the two trimers of each hexamer increased upon oxygenation by about 2.5 A. These strongly coupled movements are based on the particular hierarchical structure of the 4 x 6-mer. It also shows a concept of allosteric interaction in hierarchically assembled proteins to guarantee the involvement of all subunits of a native oligomer to establish very high Hill coefficients.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Decker, Heinz" sort="Decker, Heinz" uniqKey="Decker H" first="Heinz" last="Decker">Heinz Decker</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Hartmann, Hermann" sort="Hartmann, Hermann" uniqKey="Hartmann H" first="Hermann" last="Hartmann">Hermann Hartmann</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 003346 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 003346 | 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:12445474
|texte= All hierarchical levels are involved in conformational transitions of the 4 x 6-meric tarantula hemocyanin upon oxygenation.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:12445474" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |