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- Publisher Website: 10.1074/jbc.M605886200
- Scopus: eid_2-s2.0-33845609934
- PMID: 16905770
- WOS: WOS:000241235300040
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Article: Structures of R- and T-state Escherichia coli aspartokinase III: Mechanisms of the allosteric transition and inhibition by lysine
Title | Structures of R- and T-state Escherichia coli aspartokinase III: Mechanisms of the allosteric transition and inhibition by lysine |
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Authors | |
Issue Date | 2006 |
Publisher | American 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? |
Abstract | Aspartokinase 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 Identifier | http://hdl.handle.net/10722/171752 |
ISSN | 2020 Impact Factor: 5.157 2020 SCImago Journal Rankings: 2.361 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kotaka, M | en_US |
dc.contributor.author | Ren, J | en_US |
dc.contributor.author | Lockyer, M | en_US |
dc.contributor.author | Hawkins, AR | en_US |
dc.contributor.author | Stammers, DK | en_US |
dc.date.accessioned | 2012-10-30T06:16:48Z | - |
dc.date.available | 2012-10-30T06:16:48Z | - |
dc.date.issued | 2006 | en_US |
dc.identifier.citation | Journal Of Biological Chemistry, 2006, v. 281 n. 42, p. 31544-31552 | en_US |
dc.identifier.issn | 0021-9258 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171752 | - |
dc.description.abstract | Aspartokinase 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.language | eng | en_US |
dc.publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ | en_US |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.subject.mesh | Allosteric Regulation | en_US |
dc.subject.mesh | Allosteric Site | en_US |
dc.subject.mesh | Aspartate Kinase - Chemistry - Metabolism | en_US |
dc.subject.mesh | Binding Sites | en_US |
dc.subject.mesh | Catalytic Domain | en_US |
dc.subject.mesh | Cloning, Molecular | en_US |
dc.subject.mesh | Escherichia Coli - Enzymology | en_US |
dc.subject.mesh | Gene Expression Regulation, Bacterial | en_US |
dc.subject.mesh | Gene Expression Regulation, Enzymologic | en_US |
dc.subject.mesh | Lysine - Chemistry | en_US |
dc.subject.mesh | Models, Molecular | en_US |
dc.subject.mesh | Protein Conformation | en_US |
dc.subject.mesh | Protein Structure, Tertiary | en_US |
dc.title | Structures of R- and T-state Escherichia coli aspartokinase III: Mechanisms of the allosteric transition and inhibition by lysine | en_US |
dc.type | Article | en_US |
dc.identifier.email | Kotaka, M:masayo@hku.hk | en_US |
dc.identifier.authority | Kotaka, M=rp00293 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1074/jbc.M605886200 | en_US |
dc.identifier.pmid | 16905770 | - |
dc.identifier.scopus | eid_2-s2.0-33845609934 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-33845609934&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 281 | en_US |
dc.identifier.issue | 42 | en_US |
dc.identifier.spage | 31544 | en_US |
dc.identifier.epage | 31552 | en_US |
dc.identifier.isi | WOS:000241235300040 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Kotaka, M=6604073578 | en_US |
dc.identifier.scopusauthorid | Ren, J=7403083572 | en_US |
dc.identifier.scopusauthorid | Lockyer, M=36947976500 | en_US |
dc.identifier.scopusauthorid | Hawkins, AR=7102975292 | en_US |
dc.identifier.scopusauthorid | Stammers, DK=34573122600 | en_US |
dc.identifier.issnl | 0021-9258 | - |