3gtn
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | [[ | + | ==Crystal Structure of XynC from Bacillus subtilis 168== |
+ | <StructureSection load='3gtn' size='340' side='right' caption='[[3gtn]], [[Resolution|resolution]] 2.68Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3gtn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GTN FirstGlance]. <br> | ||
+ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU18150, xynC, ynfF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucuronoarabinoxylan_endo-1,4-beta-xylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.136 3.2.1.136] </span></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gtn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gtn RCSB], [http://www.ebi.ac.uk/pdbsum/3gtn PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gt/3gtn_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The recent biochemical characterization of the xylanases of glycosyl hydrolase family 5 (GH 5) has identified a distinctive endo mode of action, hydrolyzing the beta-1,4 xylan chain at a specific site directed by the position of an alpha-1,2-linked glucuronate moiety. Xylanase C (XynC), the GH 5 xylanase from Bacillus subtilis 168, has been cloned, overexpressed and crystallized. Initial data collection was performed and a preliminary model has been built into a low-quality 2.7 A resolution density map. The crystals belonged to the primitive monoclinic space group P2(1). Further screening identified an additive that resulted in large reproducible crystals. This larger more robust crystal form belonged to space group P2(1)2(1)2 and a resulting data set has been processed to 1.64 A resolution. This will be the second structure to be solved from this unique xylanase family and the first from a Gram-positive bacterium. This work may help to identify the structural determinants that allow the exceptional specificity of this enzyme and the role it plays in the biological depolymerization and processing of glucuronoxylan. | ||
- | + | Crystallization and crystallographic analysis of Bacillus subtilis xylanase C.,St John FJ, Godwin DK, Preston JF, Pozharski E, Hurlbert JC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):499-503. Epub 2009 Apr 24. PMID:19407387<ref>PMID:19407387</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]] | [[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]] | ||
- | [[Category: Hurlbert, J C | + | [[Category: Hurlbert, J C]] |
- | [[Category: John, F J.St | + | [[Category: John, F J.St]] |
- | [[Category: Pozharski, E | + | [[Category: Pozharski, E]] |
[[Category: Bacillus subtili]] | [[Category: Bacillus subtili]] | ||
[[Category: Carbohydrate metabolism]] | [[Category: Carbohydrate metabolism]] |
Revision as of 09:03, 8 December 2014
Crystal Structure of XynC from Bacillus subtilis 168
|
Categories: Bacillus subtilis | Glucuronoarabinoxylan endo-1,4-beta-xylanase | Hurlbert, J C | John, F J.St | Pozharski, E | Bacillus subtili | Carbohydrate metabolism | Gh 5 | Gh5 | Glucuronoxylan | Glycosidase | Glycosyl hydrolase | Glycosyl hydrolase family 5 | Hydrolase | Polysaccharide degradation | Secreted | Xylan degradation | Xylanase | Xync