View source for 6oyh


==Crystal structure of MraY bound to carbacaprazamycin==
<StructureSection load='6oyh' size='340' side='right'caption='[[6oyh]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6oyh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OYH 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]] 2.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NK4:(2~{S},5~{S},6~{S})-2-[(~{S})-[(2~{S},3~{R},4~{S},5~{R})-5-(aminomethyl)-3,4-bis(oxidanyl)oxolan-2-yl]oxy-[(2~{S},3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-6-heptadecyl-1,4-dimethyl-3-oxidanylidene-1,4-diazepane-5-carboxylic+acid'>NK4</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=6oyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oyh OCA], [https://pdbe.org/6oyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oyh RCSB], [https://www.ebi.ac.uk/pdbsum/6oyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oyh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MRAY_AQUAE MRAY_AQUAE] First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Novel antibacterial agents are needed to address the emergence of global antibiotic resistance. MraY is a promising candidate for antibiotic development because it is the target of five classes of naturally occurring nucleoside inhibitors with potent antibacterial activity. Although these natural products share a common uridine moiety, their core structures vary substantially and they exhibit different activity profiles. An incomplete understanding of the structural and mechanistic basis of MraY inhibition has hindered the translation of these compounds to the clinic. Here we present crystal structures of MraY in complex with representative members of the liposidomycin/caprazamycin, capuramycin, and mureidomycin classes of nucleoside inhibitors. Our structures reveal cryptic druggable hot spots in the shallow inhibitor binding site of MraY that were not previously appreciated. Structural analyses of nucleoside inhibitor binding provide insights into the chemical logic of MraY inhibition, which can guide novel approaches to MraY-targeted antibiotic design.

Chemical logic of MraY inhibition by antibacterial nucleoside natural products.,Mashalidis EH, Kaeser B, Terasawa Y, Katsuyama A, Kwon DY, Lee K, Hong J, Ichikawa S, Lee SY Nat Commun. 2019 Jul 2;10(1):2917. doi: 10.1038/s41467-019-10957-9. PMID:31266949<ref>PMID:31266949</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6oyh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus VF5]]
[[Category: Lama glama]]
[[Category: Large Structures]]
[[Category: Lee SY]]
[[Category: Mashalidis EH]]