2we4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{Seed}}
 +
[[Image:2we4.jpg|left|200px]]
-
The entry 2we4 is ON HOLD until Paper Publication
+
<!--
 +
The line below this paragraph, containing "STRUCTURE_2we4", creates the "Structure Box" on the page.
 +
You may change the PDB parameter (which sets the PDB file loaded into the applet)
 +
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
 +
or leave the SCENE parameter empty for the default display.
 +
-->
 +
{{STRUCTURE_2we4| PDB=2we4 | SCENE= }}
-
Authors: Ramon-Maiques, S., Marina, A., Gil-Ortiz, F., Rubio, V.
+
===CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO A SULFATE ION AND TWO WATER MOLECULES, WHICH MIMIC THE SUBSTRATE CARBAMYL PHOSPHATE===
-
Description: Carbamate kinase from Enterococcus faecalis bound to a sulfate ion and two water molecules, which mimic the substrate carbamyl phosphate
 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 25 12:49:42 2010''
+
<!--
 +
The line below this paragraph, {{ABSTRACT_PUBMED_20188742}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 20188742 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_20188742}}
 +
 
 +
==About this Structure==
 +
2WE4 is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WE4 OCA].
 +
 
 +
==Reference==
 +
<ref group="xtra">PMID:20188742</ref><ref group="xtra">PMID:10211841</ref><ref group="xtra">PMID:10860751</ref><references group="xtra"/>
 +
[[Category: Carbamate kinase]]
 +
[[Category: Enterococcus faecalis]]
 +
[[Category: Gil-Ortiz, F.]]
 +
[[Category: Marina, A.]]
 +
[[Category: Ramon-Maiques, S.]]
 +
[[Category: Rubio, V.]]
 +
[[Category: Arginine catabolism]]
 +
[[Category: Arginine metabolism]]
 +
[[Category: Atp synthesy]]
 +
[[Category: Kinase]]
 +
[[Category: Open alpha/beta sheet]]
 +
[[Category: Phosphotransferase]]
 +
[[Category: Transferase]]
 +
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 17 09:32:56 2010''

Revision as of 07:32, 17 March 2010

Image:2we4.jpg

Template:STRUCTURE 2we4

CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO A SULFATE ION AND TWO WATER MOLECULES, WHICH MIMIC THE SUBSTRATE CARBAMYL PHOSPHATE

Template:ABSTRACT PUBMED 20188742

About this Structure

2WE4 is a 4 chains structure with sequences from Enterococcus faecalis. Full crystallographic information is available from OCA.

Reference

  • 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
  • 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

Page seeded by OCA on Wed Mar 17 09:32:56 2010

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2we4"
Personal tools