View source for 8ila


==Crystal structure of LmbT from Streptomyces lincolnensis NRRL ISP-5355 in complex with substrates==
<StructureSection load='8ila' size='340' side='right'caption='[[8ila]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ila]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lincolnensis Streptomyces lincolnensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ILA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ILA 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]] 2.79&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=Q3L:(2~{S})-3-[2-[(2~{S},3~{R},4~{S},5~{R},6~{R})-6-[(1~{R},2~{R})-1-azanyl-2-oxidanyl-propyl]-3,4,5-tris(oxidanyl)oxan-2-yl]sulfanyl-1~{H}-imidazol-5-yl]-2-(trimethyl-$l^{4}-azanyl)propanoic+acid'>Q3L</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=8ila FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ila OCA], [https://pdbe.org/8ila PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ila RCSB], [https://www.ebi.ac.uk/pdbsum/8ila PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ila ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A9Y8T1_STRLN A9Y8T1_STRLN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The involvement of low-molecular-weight thiols in the biosynthesis of natural products is rarely reported. During lincomycin A biosynthesis, ergothioneine (EGT) is incorporated in the S-glycosylation catalyzed by LmbT. In contrast to the widely reported glycosylation of nitrogen and oxygen atoms, the glycosylation of sulfur atoms is less studied. In particular, the crystal structure of enzymes that glycosylate thiols on small molecules rather than peptides has not been reported. Here, we report the crystal structures of LmbT in apo form and in complex with GDP and EGT S-conjugated lincosamine. We found that LmbT has a characteristic glycosyltransferase type B fold, which forms a symmetric homotetramer. The substrates are bound deeply in the catalytic cleft. Consistent with the substrate structure, LmbT does not have the large peptide binding groove of the previously reported S-glycosyltransferase. Combined with site-directed mutagenesis, we propose a catalytic mechanism for the unusual EGT-mediated S-glycosylation in natural product biosynthesis.

Structural Basis of Low-Molecular-Weight Thiol Glycosylation in Lincomycin A Biosynthesis.,Dai Y, Cheng Y, Ding W, Qiao H, Zhang D, Zhong G, Xia M, Tao J, Sun P, Fang P, Liu W ACS Chem Biol. 2023 Jun 16;18(6):1271-1277. doi: 10.1021/acschembio.3c00185. Epub , 2023 Jun 5. PMID:37272735<ref>PMID:37272735</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ila" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces lincolnensis]]
[[Category: Dai Y]]
[[Category: Fang P]]
[[Category: Liu W]]
[[Category: Qiao H]]
[[Category: Xia M]]