This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1clx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1clx.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1clx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1clx| PDB=1clx | SCENE= }}
{{STRUCTURE_1clx| PDB=1clx | SCENE= }}
-
'''CATALYTIC CORE OF XYLANASE A'''
+
===CATALYTIC CORE OF XYLANASE A===
-
==Overview==
+
<!--
-
The three-dimensional structure of native xylanase A from Pseudomonas flouorescens subspecies cellulosa has been refined at 1.8 A resolution. The space group is P2(1)2(1)2(1) with four molecules in the asymmetric unit. The final model has an R factor of 0.166 for 103 749 reflections with the four molecules refined independently. The tertiary structure consists of an eightfold beta/alpha-barrel, the so-called TIM-barrel fold. The active site is in an open cleft at the carboxy-terminal end of the beta/alpha-barrel, and the active-site residues are a pair of glutamates, Glu127 on strand 4 and Glu246 on strand 7. Both these catalytic glutamate residues are found on beta-bulges. An atypically long loop after strand 7 is stabilized by calcium. Unusual features include a non-proline cis-peptide residue Ala80 which is found on a beta-bulge at the end of beta-strand 3. The three beta-bulge type distortions occurring on beta-strands 3, 4 and 7 are functionally significant as they serve to orient important active-site residues. The active-site residues are further held in place by an extensive hydrogen-bonding network of active-site residues in the catalytic site of xylanase A. A chain of well ordered water molecules occupies the substrate-binding cleft, some or all of which are expelled on binding of the substrate.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15299710}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15299710 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15299710}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Family-f xylanase family 10 glycosyl-hydrolase]]
[[Category: Family-f xylanase family 10 glycosyl-hydrolase]]
[[Category: Xylanase]]
[[Category: Xylanase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:52:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:55:47 2008''

Revision as of 17:55, 30 June 2008

Image:1clx.png

Template:STRUCTURE 1clx

CATALYTIC CORE OF XYLANASE A

Template:ABSTRACT PUBMED 15299710

About this Structure

1CLX is a Single protein structure of sequence from Cellvibrio japonicus. Full crystallographic information is available from OCA.

Reference

Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution., Harris GW, Jenkins JA, Connerton I, Pickersgill RW, Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):393-401. PMID:15299710

Page seeded by OCA on Mon Jun 30 20:55:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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