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2dtj

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==About this Structure==
==About this Structure==
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2DTJ is a 2 chains structure of sequences 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].
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[[2dtj]] is a 2 chain structure with 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==
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[[Category: Protein-ligand complex]]
[[Category: Protein-ligand complex]]
[[Category: Regulatory subunit]]
[[Category: Regulatory subunit]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 15:50:44 2009''
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Revision as of 18:37, 14 March 2011

Image:2dtj.png

Template:STRUCTURE 2dtj

Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum

Template:ABSTRACT PUBMED 17350037

About this Structure

2dtj is a 2 chain structure with sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA.

Reference

  • Yoshida A, Tomita T, Kurihara T, Fushinobu S, Kuzuyama T, Nishiyama M. Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum. J Mol Biol. 2007 Apr 27;368(2):521-36. Epub 2007 Feb 20. PMID:17350037 doi:10.1016/j.jmb.2007.02.017
  • Thierbach G, Kalinowski J, Bachmann B, Puhler A. Cloning of a DNA fragment from Corynebacterium glutamicum conferring aminoethyl cysteine resistance and feedback resistance to aspartokinase. Appl Microbiol Biotechnol. 1990 Jan;32(4):443-8. PMID:1366393
  • Kalinowski J, Cremer J, Bachmann B, Eggeling L, Sahm H, Puhler A. Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum. Mol Microbiol. 1991 May;5(5):1197-204. PMID:1956296
  • Kato C, Kurihara T, Kobashi N, Yamane H, Nishiyama M. Conversion of feedback regulation in aspartate kinase by domain exchange. Biochem Biophys Res Commun. 2004 Apr 9;316(3):802-8. PMID:15033471 doi:10.1016/j.bbrc.2004.02.122

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