5ngw: Difference between revisions
m Protected "5ngw" [edit=sysop:move=sysop] |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Glycoside hydrolase-like protein== | |||
<StructureSection load='5ngw' size='340' side='right'caption='[[5ngw]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ngw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ochrovirga_pacifica Ochrovirga pacifica]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5NGW 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]] 2.4Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=5ngw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ngw OCA], [https://pdbe.org/5ngw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ngw RCSB], [https://www.ebi.ac.uk/pdbsum/5ngw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ngw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2R2JFJ2_9FLAO A0A2R2JFJ2_9FLAO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Algal 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<ref>PMID:28884852</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Hehemann | <div class="pdbe-citations 5ngw" style="background-color:#fffaf0;"></div> | ||
[[Category: Robb | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ochrovirga pacifica]] | |||
[[Category: Hehemann J-H]] | |||
[[Category: Robb CS]] | |||
Latest revision as of 15:56, 15 November 2023
Glycoside hydrolase-like proteinGlycoside hydrolase-like protein
Structural highlights
FunctionPublication 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
|
| ||||||||||||||||||