2we5: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:10211841</ref><ref group="xtra">PMID:10860751</ref><references group="xtra"/> | |||
[[Category: Carbamate kinase]] | [[Category: Carbamate kinase]] | ||
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
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[[Category: Transferase]] | [[Category: Transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 7 10:01:26 2010'' | ||
Revision as of 07:01, 7 April 2010
CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADP
Template:ABSTRACT PUBMED 10211841
About this Structure
2WE5 is a 3 chains structure with sequences from Enterococcus faecalis. Full crystallographic information is available from OCA.
Reference
- 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:https://dx.doi.org/10.1006/jmbi.2000.3779
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