1clx

<table><tr><td colspan='2'>[[1clx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1CLX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRUNCATED XYNA (CODONS 264-611 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155077 "Cellvibrio cellulosa" Nagy et al. 2002])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1clx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clx OCA], [http://pdbe.org/1clx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1clx RCSB], [http://www.ebi.ac.uk/pdbsum/1clx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1clx ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15299710</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1clx" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Cellvibrio cellulosa nagy et al. 2002]]

[[Category: Endo-1,4-beta-xylanase]]

[[Category: Connerton, I]]

[[Category: Harris, G W]]

[[Category: Jenkins, J A]]

[[Category: Pickersgill, R W]]

[[Category: Xylanase]]