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]] | |||
Revision as of 11:09, 18 January 2017
MraY tunicamycin complexMraY tunicamycin complex
Structural highlights
Function[R0BTE9_9FIRM] First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan.[HAMAP-Rule:MF_00038] Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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