2dtj
From Proteopedia
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| - | [[Image:2dtj.jpg|left|200px]] | + | [[Image:2dtj.jpg|left|200px]] |
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| - | '''Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum''' | + | {{Structure |
| + | |PDB= 2dtj |SIZE=350|CAPTION= <scene name='initialview01'>2dtj</scene>, resolution 1.58Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=THR:THREONINE'>THR</scene> and <scene name='pdbligand=CIT:CITRIC ACID'>CIT</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2DTJ is a [ | + | 2DTJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DTJ OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17350037 17350037] |
[[Category: Aspartate kinase]] | [[Category: Aspartate kinase]] | ||
[[Category: Corynebacterium glutamicum]] | [[Category: Corynebacterium glutamicum]] | ||
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[[Category: regulatory subunit]] | [[Category: regulatory subunit]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:31:25 2008'' |
Revision as of 14:31, 20 March 2008
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| , resolution 1.58Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aspartate kinase, with EC number 2.7.2.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum
Overview
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 Structure
2DTJ is a Single protein structure of sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA.
Reference
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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