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1clx

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[[Image:1clx.gif|left|200px]]
 
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{{Structure
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==CATALYTIC CORE OF XYLANASE A==
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|PDB= 1clx |SIZE=350|CAPTION= <scene name='initialview01'>1clx</scene>, resolution 1.8&Aring;
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<StructureSection load='1clx' size='340' side='right'caption='[[1clx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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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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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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<table><tr><td colspan='2'>[[1clx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1CLX FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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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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<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>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1clx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clx OCA], [https://pdbe.org/1clx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1clx RCSB], [https://www.ebi.ac.uk/pdbsum/1clx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1clx ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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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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== Function ==
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}}
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[https://www.uniprot.org/uniprot/XYNA_CELJU XYNA_CELJU]
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== Evolutionary Conservation ==
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'''CATALYTIC CORE OF XYLANASE A'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/1clx_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1CLX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLX OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1clx ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15299710 15299710]
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</StructureSection>
[[Category: Cellvibrio japonicus]]
[[Category: Cellvibrio japonicus]]
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[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Connerton I]]
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[[Category: Connerton, I.]]
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[[Category: Harris GW]]
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[[Category: Harris, G W.]]
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[[Category: Jenkins JA]]
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[[Category: Jenkins, J A.]]
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[[Category: Pickersgill RW]]
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[[Category: Pickersgill, R W.]]
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[[Category: family-f xylanase family 10 glycosyl-hydrolase]]
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[[Category: xylanase]]
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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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Current revision

CATALYTIC CORE OF XYLANASE A

PDB ID 1clx

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