5jnq: Difference between revisions

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'''Unreleased structure'''


The entry 5jnq is ON HOLD
==MraY tunicamycin complex==
<StructureSection load='5jnq' size='340' side='right'caption='[[5jnq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jnq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterocloster_bolteae_90A9 Enterocloster bolteae 90A9]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5JNQ 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jnq OCA], [https://pdbe.org/5jnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jnq RCSB], [https://www.ebi.ac.uk/pdbsum/5jnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jnq ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5jnq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Enterocloster bolteae 90A9]]
[[Category: Large Structures]]
[[Category: Johansson P]]

Latest revision as of 21:59, 20 September 2023

MraY tunicamycin complexMraY tunicamycin complex

Structural highlights

5jnq is a 1 chain structure with sequence from Enterocloster bolteae 90A9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Hakulinen JK, Hering J, Branden G, Chen H, Snijder A, Ek M, Johansson P. MraY-antibiotic complex reveals details of tunicamycin mode of action. Nat Chem Biol. 2017 Jan 9. doi: 10.1038/nchembio.2270. PMID:28068312 doi:http://dx.doi.org/10.1038/nchembio.2270

5jnq, resolution 2.60Å

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