2jer
From Proteopedia
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AGMATINE DEIMINASE OF ENTEROCOCCUS FAECALIS CATALYZING ITS REACTION.
Overview
Enterococcus faecalis makes ATP from agmatine in three steps catalyzed by, agmatine deiminase (AgDI), putrescine transcarbamylase (PTC), and, carbamate kinase (CK). An antiporter exchanges putrescine for agmatine. We, have cloned the E. faecalis ef0732 and ef0734 genes of the reported gene, cluster for agmatine catabolism, overexpressed them in Escherichia coli, purified the products, characterized them functionally as PTC and AgDI, and crystallized and X-ray diffracted them. The 1.65-Angstroms-resolution, structure of AgDI forming a covalent adduct with an agmatine-derived, amidine reactional intermediate is described. We provide definitive, identification of the gene cluster for agmatine catabolism and confirm, that ornithine is a genuine but poor PTC substrate, suggesting that PTC, ... [(full description)]
About this Structure
2JER is a [Single protein] structure of sequence from [Enterococcus faecalis] with AGT and AGT as [ligands]. This structure superseeds the now removed PDB entry 2J2T. Active as [Agmatine deiminase], with EC number [3.5.3.12]. Structure known Active Site: CATALYTIC. Full crystallographic information is available from [OCA].
Reference
The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction., Llacer JL, Polo LM, Tavarez S, Alarcon B, Hilario R, Rubio V, J Bacteriol. 2007 Feb;189(4):1254-65. Epub 2006 Oct 6. PMID:17028272
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