2dtj: Difference between revisions

Revision as of 18:51, 27 July 2008

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File:2dtj.png

Template:STRUCTURE 2dtj

Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicumCrystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum

Template:ABSTRACT PUBMED 17350037

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

Cloning of a DNA fragment from Corynebacterium glutamicum conferring aminoethyl cysteine resistance and feedback resistance to aspartokinase., Thierbach G, Kalinowski J, Bachmann B, Puhler A, Appl Microbiol Biotechnol. 1990 Jan;32(4):443-8. PMID:1366393

Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum., Kalinowski J, Cremer J, Bachmann B, Eggeling L, Sahm H, Puhler A, Mol Microbiol. 1991 May;5(5):1197-204. PMID:1956296

Conversion of feedback regulation in aspartate kinase by domain exchange., Kato C, Kurihara T, Kobashi N, Yamane H, Nishiyama M, Biochem Biophys Res Commun. 2004 Apr 9;316(3):802-8. PMID:15033471

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OCA

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 {{STRUCTURE_2dtj|  PDB=2dtj  |  SCENE=  }}
-'''Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17350037}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17350037 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17350037}}
 ==About this Structure==
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 ==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://www.ncbi.nlm.nih.gov/pubmed/17350037 17350037]
+Cloning of a DNA fragment from Corynebacterium glutamicum conferring aminoethyl cysteine resistance and feedback resistance to aspartokinase., Thierbach G, Kalinowski J, Bachmann B, Puhler A, Appl Microbiol Biotechnol. 1990 Jan;32(4):443-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1366393 1366393]
+Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum., Kalinowski J, Cremer J, Bachmann B, Eggeling L, Sahm H, Puhler A, Mol Microbiol. 1991 May;5(5):1197-204. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1956296 1956296]
+Conversion of feedback regulation in aspartate kinase by domain exchange., Kato C, Kurihara T, Kobashi N, Yamane H, Nishiyama M, Biochem Biophys Res Commun. 2004 Apr 9;316(3):802-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15033471 15033471]
 [[Category: Aspartate kinase]]
 [[Category: Corynebacterium glutamicum]]
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 [[Category: Protein-ligand complex]]
 [[Category: Regulatory subunit]]
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