5y7o - Revision history

OCA at 09:12, 21 October 2020

OCA — Wed, 21 Oct 2020 09:12:49 GMT

OCA: Protected "5y7o" [edit=sysop:move=sysop]

OCA — Wed, 01 Nov 2017 06:16:45 GMT

Protected "5y7o" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:16, 1 November 2017

OCA: New page: ==Crystal structure of folding sensor region of UGGT from Thermomyces dupontii== == Structural highlights ==
<table><tr><td colspan='2'>[[5y7o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10518 Atcc 10518]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y7O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y7O FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h18|5h18]], [[5y7f|5y7f]]</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=5y7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y7o OCA], [http://pdbe.org/5y7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y7o RCSB], [http://www.ebi.ac.uk/pdbsum/5y7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y7o ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the endoplasmic reticulum (ER), a protein quality control system facilitates the efficient folding of newly synthesised proteins. In this system, a series of N-linked glycan intermediates displayed on the protein surface serve as quality tags. The ER folding-sensor enzyme UDP-glucose:glycoprotein glucosyltransferase (UGGT) acts as a gatekeeper in the ER quality control system by specifically catalysing monoglucosylation onto incompletely folded glycoproteins, thereby enabling them to interact with lectin-chaperone complexes. Here we characterise the dynamic structure of this enzyme. Our crystallographic data demonstrate that the sensor region is composed of four thioredoxin-like domains followed by a beta-rich domain, which are arranged into a C-shaped structure with a large central cavity, while the C-terminal catalytic domain undergoes a ligand-dependent conformational alteration. Furthermore, small-angle X-ray scattering, cryo-electron microscopy and high-speed atomic force microscopy have demonstrated that UGGT has a flexible modular structure in which the smaller catalytic domain is tethered to the larger folding-sensor region with variable spatial arrangements. These findings provide structural insights into the working mechanism whereby UGGT operates as a folding-sensor against a variety of glycoprotein substrates through its flexible modular structure possessing extended hydrophobic surfaces for the recognition of unfolded substrates.

Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT.,Satoh T, Song C, Zhu T, Toshimori T, Murata K, Hayashi Y, Kamikubo H, Uchihashi T, Kato K Sci Rep. 2017 Sep 22;7(1):12142. doi: 10.1038/s41598-017-12283-w. PMID:28939828<ref>PMID:28939828</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5y7o" style="background-color:#fffaf0;"></div>
== References ==
<references/>
TOC
</StructureSection>
[[Category: Atcc 10518]]
[[Category: Hayashi, Y]]
[[Category: Kamikubo, H]]
[[Category: Kato, K]]
[[Category: Murata, K]]
[[Category: Satoh, T]]
[[Category: Song, C]]
[[Category: Toshimori, T]]
[[Category: Uchihashi, T]]
[[Category: Zhu, T]]
[[Category: Endoplasmic reticulum]]
[[Category: Folding sensor]]
[[Category: Glucosyltransferase]]
[[Category: Quality control]]
[[Category: Transferase]]