5jnq: Difference between revisions
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==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]] | |||
