1clx: Difference between revisions

Revision as of 20:55, 30 June 2008

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File:1clx.png

Template:STRUCTURE 1clx

CATALYTIC CORE OF XYLANASE ACATALYTIC CORE OF XYLANASE A

Template:ABSTRACT PUBMED 15299710

About this StructureAbout this Structure

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

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1clx.gif|left|200px]]
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 {{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==
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 [[Category: Family-f xylanase family 10 glycosyl-hydrolase]]
 [[Category: Xylanase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:52:29 2008''
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