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Article: Structures of R- and T-state Escherichia coli aspartokinase III: Mechanisms of the allosteric transition and inhibition by lysine

TitleStructures of R- and T-state Escherichia coli aspartokinase III: Mechanisms of the allosteric transition and inhibition by lysine
Authors
Issue Date2006
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2006, v. 281 n. 42, p. 31544-31552 How to Cite?
AbstractAspartokinase III (AKIII) from Escherichia coli catalyzes an initial commitment step of the aspartate pathway, giving biosynthesis of certain amino acids including lysine. We report crystal structures of AKIII in the inactive T-state with bound feedback allosteric inhibitor lysine and in the R-state with aspartate and ADP. The structures reveal an unusual configuration for the regulatory ACT domains, in which ACT2 is inserted into ACT1 rather than the expected tandem repeat. Comparison of R- and T-state AKIII indicates that binding of lysine to the regulatory ACT1domain in R-state AKIII instigates a series of changes that release a "latch", the β15-αK loop, from the catalytic domain, which in turn undergoes large rotational rearrangements, promoting tetramer formation and completion of the transition to the T-state. Lysine-induced allosteric transition in AKIII involves both destabilizing the R-state and stabilizing the T-state tetramer. Rearrangement of the catalytic domain blocks the ATP-binding site, which is therefore the structural basis for allosteric inhibition of AKIII by lysine. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/171752
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKotaka, Men_US
dc.contributor.authorRen, Jen_US
dc.contributor.authorLockyer, Men_US
dc.contributor.authorHawkins, ARen_US
dc.contributor.authorStammers, DKen_US
dc.date.accessioned2012-10-30T06:16:48Z-
dc.date.available2012-10-30T06:16:48Z-
dc.date.issued2006en_US
dc.identifier.citationJournal Of Biological Chemistry, 2006, v. 281 n. 42, p. 31544-31552en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/171752-
dc.description.abstractAspartokinase III (AKIII) from Escherichia coli catalyzes an initial commitment step of the aspartate pathway, giving biosynthesis of certain amino acids including lysine. We report crystal structures of AKIII in the inactive T-state with bound feedback allosteric inhibitor lysine and in the R-state with aspartate and ADP. The structures reveal an unusual configuration for the regulatory ACT domains, in which ACT2 is inserted into ACT1 rather than the expected tandem repeat. Comparison of R- and T-state AKIII indicates that binding of lysine to the regulatory ACT1domain in R-state AKIII instigates a series of changes that release a "latch", the β15-αK loop, from the catalytic domain, which in turn undergoes large rotational rearrangements, promoting tetramer formation and completion of the transition to the T-state. Lysine-induced allosteric transition in AKIII involves both destabilizing the R-state and stabilizing the T-state tetramer. Rearrangement of the catalytic domain blocks the ATP-binding site, which is therefore the structural basis for allosteric inhibition of AKIII by lysine. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAllosteric Regulationen_US
dc.subject.meshAllosteric Siteen_US
dc.subject.meshAspartate Kinase - Chemistry - Metabolismen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCatalytic Domainen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshEscherichia Coli - Enzymologyen_US
dc.subject.meshGene Expression Regulation, Bacterialen_US
dc.subject.meshGene Expression Regulation, Enzymologicen_US
dc.subject.meshLysine - Chemistryen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.titleStructures of R- and T-state Escherichia coli aspartokinase III: Mechanisms of the allosteric transition and inhibition by lysineen_US
dc.typeArticleen_US
dc.identifier.emailKotaka, M:masayo@hku.hken_US
dc.identifier.authorityKotaka, M=rp00293en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.M605886200en_US
dc.identifier.pmid16905770-
dc.identifier.scopuseid_2-s2.0-33845609934en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33845609934&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume281en_US
dc.identifier.issue42en_US
dc.identifier.spage31544en_US
dc.identifier.epage31552en_US
dc.identifier.isiWOS:000241235300040-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridKotaka, M=6604073578en_US
dc.identifier.scopusauthoridRen, J=7403083572en_US
dc.identifier.scopusauthoridLockyer, M=36947976500en_US
dc.identifier.scopusauthoridHawkins, AR=7102975292en_US
dc.identifier.scopusauthoridStammers, DK=34573122600en_US

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