2we5: Difference between revisions

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m Protected "2we5" [edit=sysop:move=sysop]
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[[Image:2we5.png|left|200px]]
[[Image:2we5.png|left|200px]]


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{{STRUCTURE_2we5|  PDB=2we5  |  SCENE=  }}  
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===CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADP===
===CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADP===


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==Reference==
==Reference==
<ref group="xtra">PMID:10211841</ref><ref group="xtra">PMID:10860751</ref><references group="xtra"/>
<ref group="xtra">PMID:010211841</ref><ref group="xtra">PMID:010860751</ref><ref group="xtra">PMID:020188742</ref><references group="xtra"/>
[[Category: Carbamate kinase]]
[[Category: Carbamate kinase]]
[[Category: Enterococcus faecalis]]
[[Category: Enterococcus faecalis]]

Revision as of 16:12, 30 January 2013

File:2we5.png

Template:STRUCTURE 2we5

CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADPCARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADP

Template:ABSTRACT PUBMED 10211841

About this StructureAbout this Structure

2we5 is a 3 chain structure with sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1][xtra 2][xtra 3]

  1. Marina A, Alzari PM, Bravo J, Uriarte M, Barcelona B, Fita I, Rubio V. Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine. Protein Sci. 1999 Apr;8(4):934-40. PMID:10211841
  2. Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V. The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. J Mol Biol. 2000 Jun 2;299(2):463-76. PMID:10860751 doi:http://dx.doi.org/10.1006/jmbi.2000.3779
  3. Ramon-Maiques S, Marina A, Guinot A, Gil-Ortiz F, Uriarte M, Fita I, Rubio V. Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria. J Mol Biol. 2010 Apr 16;397(5):1261-75. Epub 2010 Feb 25. PMID:20188742 doi:10.1016/j.jmb.2010.02.038

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