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| - | [[Image:2jer.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2jer| PDB=2jer | SCENE= }} | | {{STRUCTURE_2jer| PDB=2jer | SCENE= }} |
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| - | '''AGMATINE DEIMINASE OF ENTEROCOCCUS FAECALIS CATALYZING ITS REACTION.'''
| + | ===AGMATINE DEIMINASE OF ENTEROCOCCUS FAECALIS CATALYZING ITS REACTION.=== |
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| - | ==Overview==
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| - | 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 (found here to be trimeric) evolved from ornithine transcarbamylase. N-(Phosphonoacetyl)-putrescine was prepared and shown to strongly (K(i) = 10 nM) and selectively inhibit PTC and to improve PTC crystallization. We find that E. faecalis AgDI, which is committed to ATP generation, closely resembles the AgDIs involved in making polyamines, suggesting the recruitment of a polyamine-synthesizing AgDI into the AgDI pathway. The arginine deiminase (ADI) pathway of arginine catabolism probably supplied the genes for PTC and CK but not those for the agmatine/putrescine antiporter, and thus the AgDI and ADI pathways are not related by a single "en bloc" duplication event. The AgDI crystal structure reveals a tetramer with a five-blade propeller subunit fold, proves that AgDI closely resembles ADI despite a lack of sequence identity, and explains substrate affinity, selectivity, and Cys357-mediated-covalent catalysis. A three-tongued agmatine-triggered gating opens or blocks access to the active center.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17028272}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17028272 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17028272}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Tetramer]] | | [[Category: Tetramer]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:47:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:45:33 2008'' |
Revision as of 03:45, 28 July 2008
Template:STRUCTURE 2jer
AGMATINE DEIMINASE OF ENTEROCOCCUS FAECALIS CATALYZING ITS REACTION.
Template:ABSTRACT PUBMED 17028272
About this Structure
2JER is a Single protein structure of sequence from Enterococcus faecalis. This structure supersedes the now removed PDB entry 2j2t. 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
Page seeded by OCA on Mon Jul 28 06:45:33 2008
