2we5

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'''Unreleased structure'''
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{{Seed}}
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[[Image:2we5.jpg|left|200px]]
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The entry 2we5 is ON HOLD until Paper Publication
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{{STRUCTURE_2we5| PDB=2we5 | SCENE= }}
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Authors: Ramon-Maiques, S., Marina, A., Rubio, V.
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===CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADP===
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Description: Carbamate kinase from Enterococcus faecalis bound to MgADP
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 25 12:49:44 2010''
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{{ABSTRACT_PUBMED_20188742}}
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==About this Structure==
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2WE5 is a 3 chains structure with sequences from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WE5 OCA].
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==Reference==
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<ref group="xtra">PMID:20188742</ref><ref group="xtra">PMID:10211841</ref><ref group="xtra">PMID:10860751</ref><references group="xtra"/>
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[[Category: Carbamate kinase]]
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[[Category: Enterococcus faecalis]]
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[[Category: Marina, A.]]
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[[Category: Ramon-Maiques, S.]]
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[[Category: Rubio, V.]]
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[[Category: Arginine catabolism]]
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[[Category: Arginine metabolism]]
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[[Category: Atp synthesy]]
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[[Category: Kinase]]
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[[Category: Open alpha/beta sheet]]
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[[Category: Phosphotransferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 17 09:24:36 2010''

Revision as of 07:24, 17 March 2010

Image:2we5.jpg

Template:STRUCTURE 2we5

CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADP

Template:ABSTRACT PUBMED 20188742

About this Structure

2WE5 is a 3 chains structure with sequences from Enterococcus faecalis. Full crystallographic information is available from OCA.

Reference

  • 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
  • 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
  • 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

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