View source for 7yp4


==Crystal structure of elaiophylin glycosyltransferase in apo-form==
<StructureSection load='7yp4' size='340' side='right'caption='[[7yp4]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yp4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._SCSIO_01934 Streptomyces sp. SCSIO 01934]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YP4 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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGR:R-1,2-PROPANEDIOL'>PGR</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=7yp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yp4 OCA], [https://pdbe.org/7yp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yp4 RCSB], [https://www.ebi.ac.uk/pdbsum/7yp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yp4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E5L4T5_9ACTN E5L4T5_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Elaiophylin (Ela), a unique 16-membered symmetric macrodiolide antibiotic, displays broad biological activity. Two rare 2-deoxy-L-fucose moieties at the ends of Ela are critical for its activity. Previously, elaiophylin glycosyltransferase (ElaGT) was identified as the enzyme that is responsible for the symmetric glycosylation of Ela, acting as a potential enzymatic tool for enhancing the diversity and activity of Ela. However, a symmetric catalytic mechanism has never been reported for a glycosyltransferase (GT). To explore the catalytic mechanism, the structure of ElaGT was determined in four forms: the apo form and Ela-bound, thymidine diphosphate-bound and uridine diphosphate-bound forms. In the Ela-bound structure, two ElaGTs form a `face-to-face' C2-symmetric homodimer with a continuous acceptor-binding pocket, allowing a molecule of Ela to shuffle through. Interestingly, this dimer interface resembles that of the activator-dependent GT EryCIII with its activator EryCII. Sequence analysis also indicates that ElaGT belongs to the activator-dependent GT family, but no putative activator has been identified in the Ela gene cluster. It was then found that the ElaGT homodimer may utilize this `face-to-face' arrangement to stabilize the Ela-binding loops on the interface and to simultaneously allosterically regulate the catalytic center. Therefore, these structures present a novel self-activating model for symmetric sugar transfer in the GT family and a new potential regulation site for substrate specificity.

Substrate-induced dimerization of elaiophylin glycosyltransferase reveals a novel self-activating form of glycosyltransferase for symmetric glycosylation.,Xu T, Gan Q, Liu Q, Chen R, Zhen X, Zhang C, Liu J Acta Crystallogr D Struct Biol. 2022 Oct 1;78(Pt 10):1235-1248. doi:, 10.1107/S2059798322008658. Epub 2022 Sep 27. PMID:36189743<ref>PMID:36189743</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yp4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. SCSIO 01934]]
[[Category: Gan Q]]
[[Category: Liu J]]
[[Category: Liu Q]]
[[Category: Xu T]]