InforLorV4, Main, Exploration, bibRecord, 003797

Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima

Identifieur interne : 003797 ( Main/Exploration ); précédent : 003796; suivant : 003798

Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima

Auteurs : James Lipchock [États-Unis] ; J. Patrick Loria [États-Unis]

Source :

Journal of biomolecular NMR [ 0925-2738 ] ; 2009.

RBID : PMC:2918893

Abstract

IGPS is a 51 kDa heterodimeric enzyme comprised of two proteins, HisH and HisF, that catalyze the hydrolysis of glutamine to produce NH₃ in the HisH active site and the cyclization of ammonia with N’-[(5’-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide (PRFAR) in HisF to produce imidazole glycerol phosphate (IGP) and 5-aminoimidazole-4-carboxamide ribotide (AICAR). Binding of PRFAR and IGP stimulates glutaminase activity in the HisH enzyme over 5000 and 100-fold, respectively, despite the active sites being > 25 Å apart. The details of this long-range protein communication process were investigated by solution NMR spectroscopy and CPMG relaxation dispersion experiments. Formation of the heterodimer enzyme results in a reduction in millisecond motions in HisF that extend throughout the protein. Binding of lGP results in an increase in protein-wide millisecond dynamics evidenced as severe NMR line broadening. Together, these data demonstrate a grouping of flexible residues that link the HisF active site with the protein interface to which HisH binds and provide a model for the path of communication between the IGPS active sites.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2918893

DOI: 10.1007/s10858-009-9337-8
PubMed: 19565337
PubMed Central: 2918893

Affiliations:

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from <italic>Thermotoga maritima</italic>
</title>
<author><name sortKey="Lipchock, James" sort="Lipchock, James" uniqKey="Lipchock J" first="James" last="Lipchock">James Lipchock</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Chemistry, Yale University, New Haven, CT 06520</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Connecticut</region>
</placeName>
<wicri:cityArea>Department of Chemistry, Yale University, New Haven</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Loria, J Patrick" sort="Loria, J Patrick" uniqKey="Loria J" first="J. Patrick" last="Loria">J. Patrick Loria</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Chemistry, Yale University, New Haven, CT 06520</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Connecticut</region>
</placeName>
<wicri:cityArea>Department of Chemistry, Yale University, New Haven</wicri:cityArea>
</affiliation>
<affiliation wicri:level="2"><nlm:aff id="A2">Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Connecticut</region>
</placeName>
<wicri:cityArea>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven</wicri:cityArea>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">19565337</idno>
<idno type="pmc">2918893</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2918893</idno>
<idno type="RBID">PMC:2918893</idno>
<idno type="doi">10.1007/s10858-009-9337-8</idno>
<date when="2009">2009</date>
<idno type="wicri:Area/Pmc/Corpus">000048</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000048</idno>
<idno type="wicri:Area/Pmc/Curation">000048</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000048</idno>
<idno type="wicri:Area/Pmc/Checkpoint">000077</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000077</idno>
<idno type="wicri:Area/Ncbi/Merge">000082</idno>
<idno type="wicri:Area/Ncbi/Curation">000080</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000080</idno>
<idno type="wicri:doubleKey">0925-2738:2009:Lipchock J:millisecond:dynamics:in</idno>
<idno type="wicri:Area/Main/Merge">003874</idno>
<idno type="wicri:Area/Main/Curation">003797</idno>
<idno type="wicri:Area/Main/Exploration">003797</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from <italic>Thermotoga maritima</italic>
</title>
<author><name sortKey="Lipchock, James" sort="Lipchock, James" uniqKey="Lipchock J" first="James" last="Lipchock">James Lipchock</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Chemistry, Yale University, New Haven, CT 06520</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Connecticut</region>
</placeName>
<wicri:cityArea>Department of Chemistry, Yale University, New Haven</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Loria, J Patrick" sort="Loria, J Patrick" uniqKey="Loria J" first="J. Patrick" last="Loria">J. Patrick Loria</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Chemistry, Yale University, New Haven, CT 06520</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Connecticut</region>
</placeName>
<wicri:cityArea>Department of Chemistry, Yale University, New Haven</wicri:cityArea>
</affiliation>
<affiliation wicri:level="2"><nlm:aff id="A2">Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Connecticut</region>
</placeName>
<wicri:cityArea>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven</wicri:cityArea>
</affiliation>
</author>
</analytic>
<series><title level="j">Journal of biomolecular NMR</title>
<idno type="ISSN">0925-2738</idno>
<idno type="eISSN">1573-5001</idno>
<imprint><date when="2009">2009</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p id="P1">IGPS is a 51 kDa heterodimeric enzyme comprised of two proteins, HisH and HisF, that catalyze the hydrolysis of glutamine to produce NH<sub>3</sub>
 in the HisH active site and the cyclization of ammonia with N’-[(5’-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide (PRFAR) in HisF to produce imidazole glycerol phosphate (IGP) and 5-aminoimidazole-4-carboxamide ribotide (AICAR). Binding of PRFAR and IGP stimulates glutaminase activity in the HisH enzyme over 5000 and 100-fold, respectively, despite the active sites being > 25 Å apart. The details of this long-range protein communication process were investigated by solution NMR spectroscopy and CPMG relaxation dispersion experiments. Formation of the heterodimer enzyme results in a reduction in millisecond motions in HisF that extend throughout the protein. Binding of lGP results in an increase in protein-wide millisecond dynamics evidenced as severe NMR line broadening. Together, these data demonstrate a grouping of flexible residues that link the HisF active site with the protein interface to which HisH binds and provide a model for the path of communication between the IGPS active sites.</p>
</div>
</front>
</TEI>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Connecticut</li>
</region>
</list>
<tree><country name="États-Unis"><region name="Connecticut"><name sortKey="Lipchock, James" sort="Lipchock, James" uniqKey="Lipchock J" first="James" last="Lipchock">James Lipchock</name>
</region>
<name sortKey="Loria, J Patrick" sort="Loria, J Patrick" uniqKey="Loria J" first="J. Patrick" last="Loria">J. Patrick Loria</name>
<name sortKey="Loria, J Patrick" sort="Loria, J Patrick" uniqKey="Loria J" first="J. Patrick" last="Loria">J. Patrick Loria</name>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Lorraine/explor/InforLorV4/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003797 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 003797 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Lorraine
   |area=    InforLorV4
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     PMC:2918893
   |texte=   Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:19565337" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a InforLorV4

This area was generated with Dilib version V0.6.33.
Data generation: Mon Jun 10 21:56:28 2019. Site generation: Fri Feb 25 15:29:27 2022

Serveur d'exploration sur la recherche en informatique en Lorraine

Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima

Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima

Source :

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

	Serveur d'exploration sur la recherche en informatique en Lorraine
	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.