5jbq

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'''Unreleased structure'''
 
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The entry 5jbq is ON HOLD
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==EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH THIOMURACIN ANALOG==
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<StructureSection load='5jbq' size='340' side='right' caption='[[5jbq]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5jbq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JBQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JBQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=05N:(3R,4R)-4-HYDROXY-3-METHYL-L-PROLINE'>05N</scene>, <scene name='pdbligand=6RK:4-AZANYLCYCLOHEXANE-1-CARBOXYLIC+ACID'>6RK</scene>, <scene name='pdbligand=BB6:(2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC+ACID'>BB6</scene>, <scene name='pdbligand=BB9:(2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC+ACID'>BB9</scene>, <scene name='pdbligand=H14:(2S,3R)-BETA-HYDROXY-PHENYLALANINE'>H14</scene>, <scene name='pdbligand=MH6:3-HYDROXY-2-IMINOPROPANOIC+ACID'>MH6</scene></td></tr>
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<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=5jbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jbq OCA], [http://pdbe.org/5jbq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jbq RCSB], [http://www.ebi.ac.uk/pdbsum/5jbq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jbq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/EFTU1_ECOLI EFTU1_ECOLI]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Synthetic studies of the antimicrobial secondary metabolite thiomuracin A (1) provided access to analogues in the Northern region (C2-C10). Selective hydrolysis of the C10 amide of lead compound 2 and subsequent derivatization led to novel carbon- and nitrogen-linked analogues (e.g., 3) which improved antibacterial potency across a panel of Gram-positive organisms. In addition, congeners with improved physicochemical properties were identified which proved efficacious in murine sepsis and hamster C. difficile models of disease. Optimal efficacy in the hamster model of C. difficile was achieved with compounds that possessed both potent antibacterial activity and high aqueous solubility.
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Authors:
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Antibacterial and Solubility Optimization of Thiomuracin A.,LaMarche MJ, Leeds JA, Brewer J, Dean K, Ding J, Dzink-Fox J, Gamber G, Jain A, Kerrigan R, Krastel P, Lee K, Lombardo F, McKenney D, Neckermann G, Osborne C, Palestrant D, Patane MA, Rann EM, Robinson Z, Schmitt E, Stams T, Tiamfook S, Yu D, Whitehead L J Med Chem. 2016 Jul 12. PMID:27355833<ref>PMID:27355833</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5jbq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Palestrant, D]]
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[[Category: Stams, T]]
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[[Category: Elongation factor]]
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[[Category: Natural product inhibitor]]
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[[Category: Rna binding protein-antimicrobial complex]]

Revision as of 11:46, 14 July 2016

EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH THIOMURACIN ANALOG

5jbq, resolution 2.01Å

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