6oz6
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6oz6' size='340' side='right'caption='[[6oz6]], [[Resolution|resolution]] 3.70Å' scene=''> | <StructureSection load='6oz6' size='340' side='right'caption='[[6oz6]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6oz6]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OZ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6oz6]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae] and [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OZ6 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NKD:(2~{S})-2-[[(2~{S})-1-[[(2~{S},3~{S})-3-[[(2~{S})-2-azanyl-3-(3-hydroxyphenyl)propanoyl]-methyl-amino]-1-[[(~{Z})-[(3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-ylidene]methyl]amino]-1-oxidanylidene-butan-2-yl]amino]-4-methylsulfanyl-1-oxidanylidene-butan-2-yl]carbamoylamino]-3-(3-hydroxyphenyl)propanoic+acid'>NKD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NKD:(2~{S})-2-[[(2~{S})-1-[[(2~{S},3~{S})-3-[[(2~{S})-2-azanyl-3-(3-hydroxyphenyl)propanoyl]-methyl-amino]-1-[[(~{Z})-[(3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-ylidene]methyl]amino]-1-oxidanylidene-butan-2-yl]amino]-4-methylsulfanyl-1-oxidanylidene-butan-2-yl]carbamoylamino]-3-(3-hydroxyphenyl)propanoic+acid'>NKD</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mraY, aq_053 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospho-N-acetylmuramoyl-pentapeptide-transferase Phospho-N-acetylmuramoyl-pentapeptide-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.13 2.7.8.13] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospho-N-acetylmuramoyl-pentapeptide-transferase Phospho-N-acetylmuramoyl-pentapeptide-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.13 2.7.8.13] </span></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=6oz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oz6 OCA], [http://pdbe.org/6oz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oz6 RCSB], [http://www.ebi.ac.uk/pdbsum/6oz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oz6 ProSAT]</span></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=6oz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oz6 OCA], [http://pdbe.org/6oz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oz6 RCSB], [http://www.ebi.ac.uk/pdbsum/6oz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oz6 ProSAT]</span></td></tr> | ||
| Line 10: | Line 11: | ||
== Function == | == Function == | ||
[[http://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). | [[http://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6oz6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Aquae]] | ||
| + | [[Category: Camelus glama]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Phospho-N-acetylmuramoyl-pentapeptide-transferase]] | [[Category: Phospho-N-acetylmuramoyl-pentapeptide-transferase]] | ||
Revision as of 12:43, 17 July 2019
Crystal structure of MraY bound to 3'-hydroxymureidomycin A
| |||||||||||
