Nanometer propagation of millisecond motions in V-type allostery
Identifieur interne : 002F24 ( Main/Exploration ); précédent : 002F23; suivant : 002F25Nanometer propagation of millisecond motions in V-type allostery
Auteurs : James Lipchock [États-Unis] ; J. Patrick Loria [États-Unis]Source :
- Structure (London, England : 1993) [ 0969-2126 ] ; 2010.
Abstract
Imidazole glycerol phosphate synthase (IGPS) is a V-type allosteric enzyme, which is catalytically inactive for glutamine hydrolysis until the allosteric effector, N’-[(5′-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide (PRFAR) binds 30 Å away. In the apo state, NMR relaxation dispersion experiments indicate the absence of millisecond (ms) timescale motions. Binding of the PRFAR to form the active ternary complex is endothermic with a large positive entropy change. In addition, there is a protein wide enhancement of conformational motions in the ternary complex, which connect to two active sites. NMR chemical shift changes and acrylamide quenching experiments suggest that little in the way of structural changes accompany these motions. The data indicate that enzyme activation in the ternary complex is primarily due to an enhancement of ms motions that allows formation of a population of enzymatically active conformers.
Url:
DOI: 10.1016/j.str.2010.09.020
PubMed: 21134639
PubMed Central: 3003306
Affiliations:
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Patrick" last="Loria">J. Patrick Loria</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Chemistry, Yale University, New Haven, CT 06520, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Yale University, New Haven, CT 06520</wicri:regionArea><placeName><region type="state">Connecticut</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A2">Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520</wicri:regionArea><placeName><region type="state">Connecticut</region></placeName></affiliation></author></analytic><series><title level="j">Structure (London, England : 1993)</title><idno type="ISSN">0969-2126</idno><idno type="eISSN">1878-4186</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Summary</title><p id="P1">Imidazole glycerol phosphate synthase (IGPS) is a V-type allosteric enzyme, which is catalytically inactive for glutamine hydrolysis until the allosteric effector, N’-[(5′-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide (PRFAR) binds 30 Å away. In the apo state, NMR relaxation dispersion experiments indicate the absence of millisecond (ms) timescale motions. Binding of the PRFAR to form the active ternary complex is endothermic with a large positive entropy change. In addition, there is a protein wide enhancement of conformational motions in the ternary complex, which connect to two active sites. NMR chemical shift changes and acrylamide quenching experiments suggest that little in the way of structural changes accompany these motions. The data indicate that enzyme activation in the ternary complex is primarily due to an enhancement of ms motions that allows formation of a population of enzymatically active conformers.</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)
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