2jer

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2jer.gif|left|200px]]
[[Image:2jer.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2jer |SIZE=350|CAPTION= <scene name='initialview01'>2jer</scene>, resolution 1.65&Aring;
+
The line below this paragraph, containing "STRUCTURE_2jer", creates the "Structure Box" on the page.
-
|SITE= <scene name='pdbsite=CATALYTIC:The+Previous+Residues+Are+The+Residues+w.+Decreased+Acce+...'>CATALYTIC</scene>
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=AGT:S-{(S)-AMINO[(4-AMINOBUTYL)AMINO]METHYL}-L-CYSTEINE'>AGT</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Agmatine_deiminase Agmatine deiminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.12 3.5.3.12] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2jer| PDB=2jer | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jer OCA], [http://www.ebi.ac.uk/pdbsum/2jer PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jer RCSB]</span>
+
-
}}
+
'''AGMATINE DEIMINASE OF ENTEROCOCCUS FAECALIS CATALYZING ITS REACTION.'''
'''AGMATINE DEIMINASE OF ENTEROCOCCUS FAECALIS CATALYZING ITS REACTION.'''
Line 19: Line 16:
==About this Structure==
==About this Structure==
-
2JER is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. This structure supersedes the now removed PDB entry 2J2T. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JER OCA].
+
2JER is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2j2t 2j2t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JER OCA].
==Reference==
==Reference==
Line 30: Line 27:
[[Category: Tavarez, S.]]
[[Category: Tavarez, S.]]
[[Category: 5-fold pseudosymmetric structure]]
[[Category: 5-fold pseudosymmetric structure]]
-
[[Category: agdi]]
+
[[Category: Agdi]]
-
[[Category: agmatine degradation pathway]]
+
[[Category: Agmatine degradation pathway]]
-
[[Category: agmatine deiminase]]
+
[[Category: Agmatine deiminase]]
-
[[Category: agmatine iminohydrolase]]
+
[[Category: Agmatine iminohydrolase]]
-
[[Category: covalent amidino adduct]]
+
[[Category: Covalent amidino adduct]]
-
[[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 Mar 31 03:57:08 2008''
+

Revision as of 05:47, 4 May 2008

Template:STRUCTURE 2jer

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 (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.

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 Sun May 4 08:47:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools