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1nq6

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[[Image:1nq6.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8==
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|PDB= 1nq6 |SIZE=350|CAPTION= <scene name='initialview01'>1nq6</scene>, resolution 1.78&Aring;
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<StructureSection load='1nq6' size='340' side='right'caption='[[1nq6]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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<table><tr><td colspan='2'>[[1nq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_halstedii Streptomyces halstedii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NQ6 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]] 1.78&#8491;</td></tr>
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|GENE= xysA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1944 Streptomyces halstedii])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1nq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nq6 OCA], [https://pdbe.org/1nq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1nq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nq6 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=1nq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nq6 OCA], [http://www.ebi.ac.uk/pdbsum/1nq6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nq6 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q59922_STRHA Q59922_STRHA]
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== Evolutionary Conservation ==
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'''Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8'''
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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/nq/1nq6_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1nq6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Xylanases hydrolyze the beta-1,4-linked xylose backbone of xylans. They are of increasing interest in the paper and food industries for their pre-bleaching and bio-pulping applications. Such industries demand new xylanases to cover a wider range of cleavage specificity, activity and stability. The catalytic domain of xylanase Xys1 from Streptomyces halstedii JM8 was expressed, purified and crystallized and native data were collected to 1.78 A resolution with an R(merge) of 4.4%. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.05, b = 79.60, c = 87.80 A. The structure was solved by the molecular-replacement method using the structure of the homologue Xyl10A from Streptomyces lividans. In a similar manner to other members of its family, Xys1 folds to form a standard (beta/alpha)(8) barrel with the two catalytic functions, the acid/base and the nucleophile, at its C-terminal side. The overall structure is described and compared with those of related xylanases.
Xylanases hydrolyze the beta-1,4-linked xylose backbone of xylans. They are of increasing interest in the paper and food industries for their pre-bleaching and bio-pulping applications. Such industries demand new xylanases to cover a wider range of cleavage specificity, activity and stability. The catalytic domain of xylanase Xys1 from Streptomyces halstedii JM8 was expressed, purified and crystallized and native data were collected to 1.78 A resolution with an R(merge) of 4.4%. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.05, b = 79.60, c = 87.80 A. The structure was solved by the molecular-replacement method using the structure of the homologue Xyl10A from Streptomyces lividans. In a similar manner to other members of its family, Xys1 folds to form a standard (beta/alpha)(8) barrel with the two catalytic functions, the acid/base and the nucleophile, at its C-terminal side. The overall structure is described and compared with those of related xylanases.
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==About this Structure==
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Structure of xylanase Xys1delta from Streptomyces halstedii.,Canals A, Vega MC, Gomis-Ruth FX, Diaz M, Santamaria R RI, Coll M Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1447-53. Epub 2003, Jul 23. PMID:12876348<ref>PMID:12876348</ref>
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1NQ6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_halstedii Streptomyces halstedii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQ6 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of xylanase Xys1delta from Streptomyces halstedii., Canals A, Vega MC, Gomis-Ruth FX, Diaz M, Santamaria R RI, Coll M, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1447-53. Epub 2003, Jul 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12876348 12876348]
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</div>
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[[Category: Endo-1,4-beta-xylanase]]
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<div class="pdbe-citations 1nq6" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces halstedii]]
[[Category: Streptomyces halstedii]]
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[[Category: Canals, A.]]
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[[Category: Canals A]]
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[[Category: Coll, M.]]
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[[Category: Coll M]]
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[[Category: Gomis-Ruth, F X.]]
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[[Category: Gomis-Ruth FX]]
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[[Category: Santamaria, R I.]]
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[[Category: Santamaria RI]]
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[[Category: Vega, M C.]]
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[[Category: Vega MC]]
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[[Category: glycoside hydrolase family 10]]
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[[Category: xylan degradation,]]
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[[Category: xylanase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:33:57 2008''
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Current revision

Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8

PDB ID 1nq6

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