View source for 7zlg


==Cryo-EM structure of C-mannosyltransferase CeDPY19, in complex with acceptor peptide and bound to CMT2-Fab and anti-Fab nanobody==
<StructureSection load='7zlg' size='340' side='right'caption='[[7zlg]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7zlg]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZLG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.72&#8491;</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=7zlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zlg OCA], [https://pdbe.org/7zlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zlg RCSB], [https://www.ebi.ac.uk/pdbsum/7zlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zlg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7Z3Y4_HUMAN Q7Z3Y4_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
C-linked glycosylation is essential for the trafficking, folding and function of secretory and transmembrane proteins involved in cellular communication processes. The tryptophan C-mannosyltransferase (CMT) enzymes that install the modification attach a mannose to the first tryptophan of WxxW/C sequons in nascent polypeptide chains by an unknown mechanism. Here, we report cryogenic-electron microscopy structures of Caenorhabditis elegans CMT in four key states: apo, acceptor peptide-bound, donor-substrate analog-bound and as a trapped ternary complex with both peptide and a donor-substrate mimic bound. The structures indicate how the C-mannosylation sequon is recognized by this CMT and its paralogs, and how sequon binding triggers conformational activation of the donor substrate: a process relevant to all glycosyltransferase C superfamily enzymes. Our structural data further indicate that the CMTs adopt an unprecedented electrophilic aromatic substitution mechanism to enable the C-glycosylation of proteins. These results afford opportunities for understanding human disease and therapeutic targeting of specific CMT paralogs.

Structure, sequon recognition and mechanism of tryptophan C-mannosyltransferase.,Bloch JS, John A, Mao R, Mukherjee S, Boilevin J, Irobalieva RN, Darbre T, Scott NE, Reymond JL, Kossiakoff AA, Goddard-Borger ED, Locher KP Nat Chem Biol. 2023 May;19(5):575-584. doi: 10.1038/s41589-022-01219-9. Epub 2023 , Jan 5. PMID:36604564<ref>PMID:36604564</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7zlg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Bloch JS]]
[[Category: Goddard-Borger ED]]
[[Category: Irobalieva R]]
[[Category: Kossiakoff AA]]
[[Category: Locher KP]]
[[Category: Mao R]]
[[Category: Mukherjee S]]