2dtj: Difference between revisions
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|PDB= 2dtj |SIZE=350|CAPTION= <scene name='initialview01'>2dtj</scene>, resolution 1.58Å | |PDB= 2dtj |SIZE=350|CAPTION= <scene name='initialview01'>2dtj</scene>, resolution 1.58Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2dt9|2DT9]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dtj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dtj OCA], [http://www.ebi.ac.uk/pdbsum/2dtj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dtj RCSB]</span> | |||
}} | }} | ||
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[[Category: Tomita, T.]] | [[Category: Tomita, T.]] | ||
[[Category: Yoshida, A.]] | [[Category: Yoshida, A.]] | ||
[[Category: protein-ligand complex]] | [[Category: protein-ligand complex]] | ||
[[Category: regulatory subunit]] | [[Category: regulatory subunit]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:39:15 2008'' | ||
Revision as of 02:39, 31 March 2008
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| , resolution 1.58Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Aspartate kinase, with EC number 2.7.2.4 | ||||||
| Related: | 2DT9
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum
OverviewOverview
Aspartate kinase (AK) catalyzes the first step of the biosynthesis of the aspartic acid family amino acids, and is regulated via feedback inhibition by end-products including Thr and Lys. To elucidate the mechanism of this inhibition, we determined the crystal structure of the regulatory subunit of AK from Corynebacterium glutamicum at 1.58 A resolution in the Thr-binding form, the first crystal structure of the regulatory subunit of alpha(2)beta(2)-type AK. The regulatory subunit contains two ACT domain motifs per monomer and is arranged as a dimer. Two non-equivalent ACT domains from different chains form an effector-binding unit that binds a single Thr molecule, and the resulting two effector-binding units of the dimer associate perpendicularly in a face-to-face manner. The regulatory subunit is a monomer in the absence of Thr but becomes a dimer by adding Thr. The dimerization is eliminated in mutant AKs with changes in the Thr-binding region, suggesting that the dimerization induced by Thr binding is a key step in the inhibitory mechanism of AK from C. glutamicum. A putative Lys-binding site and the inhibitory mechanism of CgAK are discussed.
About this StructureAbout this Structure
2DTJ is a Single protein structure of sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA.
ReferenceReference
Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum., Yoshida A, Tomita T, Kurihara T, Fushinobu S, Kuzuyama T, Nishiyama M, J Mol Biol. 2007 Apr 27;368(2):521-36. Epub 2007 Feb 20. PMID:17350037
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