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3m4f
From Proteopedia
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| - | {{STRUCTURE_3m4f| PDB=3m4f | SCENE= }} | ||
| - | ===Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum=== | ||
| - | {{ABSTRACT_PUBMED_20621155}} | ||
| - | == | + | ==Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum== |
| - | [[3m4f]] is a 4 chain structure with sequence from [ | + | <StructureSection load='3m4f' size='340' side='right'caption='[[3m4f]], [[Resolution|resolution]] 1.89Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3m4f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidomyces_acidophilus Acidomyces acidophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M4F FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m4f OCA], [https://pdbe.org/3m4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m4f RCSB], [https://www.ebi.ac.uk/pdbsum/3m4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m4f ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6VAY1_9PEZI Q6VAY1_9PEZI] | ||
| + | == 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/m4/3m4f_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=3m4f ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In this study, the crystal structure of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum, XYL1, was solved at 1.9A resolution. This is one of the few solved crystal structures of acidophilic proteins. The enzyme has the overall fold typical to family 11 xylanases. Comparison of this structure with other homologous acidophilic, neutrophilic and alkalophilic xylanases provides additional insights into the general features involved in low pH adaptation (stability and activity). Several sequence and structure modifications appeared to be responsible for the acidophilic characteristic: (a) the presence of an aspartic acid H bonded to the acid/base catalyst (b) the nature of specifically conserved residues in the active site (c) the negative potential at the surface (d) the decreased number of salt bridges and H bonds in comparison with highly alkaline enzymes. | ||
| - | + | Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum.,Michaux C, Pouyez J, Mayard A, Vandurm P, Housen I, Wouters J Biochimie. 2010 Jul 16. PMID:20621155<ref>PMID:20621155</ref> | |
| - | <ref | + | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3m4f" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Acidomyces acidophilus]] | [[Category: Acidomyces acidophilus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Michaux | + | [[Category: Michaux C]] |
| - | [[Category: Wouters | + | [[Category: Wouters J]] |
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Current revision
Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum
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