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1clx

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[[Image:1clx.gif|left|200px]]
[[Image:1clx.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1clx |SIZE=350|CAPTION= <scene name='initialview01'>1clx</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1clx", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=CAT:Two+Catalytic+Residues+Acid-Base+GLU+127+Nucleophile+GLU+246'>CAT</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= TRUNCATED XYNA (CODONS 264-611 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155077 Cellvibrio japonicus])
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-->
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|DOMAIN=
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{{STRUCTURE_1clx| PDB=1clx | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1clx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clx OCA], [http://www.ebi.ac.uk/pdbsum/1clx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1clx RCSB]</span>
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}}
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'''CATALYTIC CORE OF XYLANASE A'''
'''CATALYTIC CORE OF XYLANASE A'''
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[[Category: Jenkins, J A.]]
[[Category: Jenkins, J A.]]
[[Category: Pickersgill, R W.]]
[[Category: Pickersgill, R W.]]
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[[Category: family-f xylanase family 10 glycosyl-hydrolase]]
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[[Category: Family-f xylanase family 10 glycosyl-hydrolase]]
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[[Category: xylanase]]
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[[Category: Xylanase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:52:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:09 2008''
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Revision as of 09:52, 2 May 2008

Template:STRUCTURE 1clx

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.

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 Fri May 2 12:52:29 2008

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