5ngw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5ngw" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5ngw is ON HOLD until Paper Publication
+
==Glycoside hydrolase-like protein==
 +
<StructureSection load='5ngw' size='340' side='right' caption='[[5ngw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== 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://oca.weizmann.ac.il/oca-docs/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>
 +
<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=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>
 +
<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.
-
Authors: Robb, C.S., Hehemann, J.-H.
+
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>
-
Description: Glycoside hydrolase-like protein
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Hehemann, J.-H]]
+
<div class="pdbe-citations 5ngw" style="background-color:#fffaf0;"></div>
-
[[Category: Robb, C.S]]
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Hehemann, J H]]
 +
[[Category: Robb, C S]]
 +
[[Category: Flavobacteria]]
 +
[[Category: Glycoside hydrolase]]
 +
[[Category: Hydrolase]]
 +
[[Category: Marine polysaccharide]]

Revision as of 05:49, 31 January 2018

Glycoside hydrolase-like protein

5ngw, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools