5jnq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==MraY tunicamycin complex== | |
| + | <StructureSection load='5jnq' size='340' side='right' caption='[[5jnq]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jnq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JNQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=TUM:TUNICAMYCIN'>TUM</scene></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=5jnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jnq OCA], [http://pdbe.org/5jnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jnq RCSB], [http://www.ebi.ac.uk/pdbsum/5jnq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jnq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/R0BTE9_9FIRM R0BTE9_9FIRM]] First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan.[HAMAP-Rule:MF_00038] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The rapid increase of antibiotic resistance has created an urgent need to develop novel antimicrobial agents. Here we describe the crystal structure of the promising bacterial target phospho-N-acetylmuramoyl-pentapeptide translocase (MraY) in complex with the nucleoside antibiotic tunicamycin. The structure not only reveals the mode of action of several related natural-product antibiotics but also gives an indication on the binding mode of the MraY UDP-MurNAc-pentapeptide and undecaprenyl-phosphate substrates. | ||
| - | + | MraY-antibiotic complex reveals details of tunicamycin mode of action.,Hakulinen JK, Hering J, Branden G, Chen H, Snijder A, Ek M, Johansson P Nat Chem Biol. 2017 Jan 9. doi: 10.1038/nchembio.2270. PMID:28068312<ref>PMID:28068312</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5jnq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Phospho-N-acetylmuramoyl-pentapeptide-transferase]] | ||
| + | [[Category: Johansson, P]] | ||
| + | [[Category: Antibiotic]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Pnpt]] | ||
| + | [[Category: Transferase-antibiotic complex]] | ||
Revision as of 08:09, 18 January 2017
MraY tunicamycin complex
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