5ngw: Difference between revisions
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==Glycoside hydrolase-like protein== | ==Glycoside hydrolase-like protein== | ||
<StructureSection load='5ngw' size='340' side='right' caption='[[5ngw]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='5ngw' size='340' side='right'caption='[[5ngw]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ngw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NGW OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5ngw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NGW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NGW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ngw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ngw OCA], [http://pdbe.org/5ngw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ngw RCSB], [http://www.ebi.ac.uk/pdbsum/5ngw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ngw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Hehemann, J H]] | [[Category: Hehemann, J H]] | ||
[[Category: Robb, C S]] | [[Category: Robb, C S]] |
Revision as of 15:04, 26 August 2020
Glycoside hydrolase-like proteinGlycoside hydrolase-like protein
Structural highlights
Publication Abstract from PubMedAlgal polysaccharides of diverse structures are one of the most abundant carbon resources for heterotrophic, marine bacteria with coevolved digestive enzymes. A putative sulfo-mannan polysaccharide utilization locus, which is conserved in marine flavobacteria, contains an unusual GH99-like protein that lacks the conserved catalytic residues of glycoside hydrolase family 99. Using X-ray crystallography, we structurally characterized this protein from the marine flavobacterium Ochrovirga pacifica to help elucidate its molecular function. The structure reveals the absence of potential catalytic residues for polysaccharide hydrolysis, which-together with additional structural features-suggests this protein may be noncatalytic and involved in carbohydrate binding. Crystal structure of a marine glycoside hydrolase family 99-related protein lacking catalytic machinery.,Robb CS, Mystkowska AA, Hehemann JH Protein Sci. 2017 Dec;26(12):2445-2450. doi: 10.1002/pro.3291. Epub 2017 Nov 21. PMID:28884852[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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