We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1js1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1js1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1js1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1js1| PDB=1js1 | SCENE= }}
{{STRUCTURE_1js1| PDB=1js1 | SCENE= }}
-
'''Crystal Structure of a new transcarbamylase from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution'''
+
===Crystal Structure of a new transcarbamylase from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution===
-
==Overview==
+
<!--
-
A transcarbamylase-like protein essential for arginine biosynthesis in the anaerobic bacterium Bacteroides fragilis has been purified and crystallized in space group P4(3)2(1)2 (a=b=153.4 A, c=94.8 A). The structure was solved using a single isomorphous replacement with anomalous scattering (SIRAS) and was refined at 2.0 A resolution to an R-factor of 20.6% (R-free=25.2%). The molecular model is trimeric and comprises 960 amino acid residues, two phosphate groups and 422 water molecules. The monomer has the consensus transcarbamylase fold with two structural domains linked by two long interdomain helices: the putative carbamoyl phosphate-binding domain and a binding domain for the second substrate. Each domain has a central parallel beta-sheet surrounded by alpha-helices and loops with alpha/beta topology. The putative carbamoyl phosphate-binding site is similar to those in ornithine transcarbamylases (OTCases) and aspartate transcarbamylases (ATCases); however, the second substrate-binding site is strikingly different. This site has several insertions and deletions, and residues critical to substrate binding and catalysis in other known transcarbamylases are not conserved. The three-dimensional structure and the fact that this protein is essential for arginine biosynthesis suggest strongly that it is a new member of the transcarbamylase family. A similar protein has been found in Xylella fastidiosa, a bacterium that infects grapes, citrus and other plants.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12095263}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12095263 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12095263}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Alpha/beta topology]]
[[Category: Alpha/beta topology]]
[[Category: Two domain]]
[[Category: Two domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:48:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:43:03 2008''

Revision as of 17:43, 1 July 2008

Image:1js1.png

Template:STRUCTURE 1js1

Crystal Structure of a new transcarbamylase from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution

Template:ABSTRACT PUBMED 12095263

About this Structure

1JS1 is a Single protein structure of sequence from Bacteroides fragilis. Full crystallographic information is available from OCA.

Reference

Crystal structure of a transcarbamylase-like protein from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution., Shi D, Gallegos R, DePonte J 3rd, Morizono H, Yu X, Allewell NM, Malamy M, Tuchman M, J Mol Biol. 2002 Jul 19;320(4):899-908. PMID:12095263

Page seeded by OCA on Tue Jul 1 20:43:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1js1"
Personal tools