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
- ↑ 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
- ↑ 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