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| | <StructureSection load='5jbq' size='340' side='right'caption='[[5jbq]], [[Resolution|resolution]] 2.01Å' scene=''> | | <StructureSection load='5jbq' size='340' side='right'caption='[[5jbq]], [[Resolution|resolution]] 2.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jbq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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://proteopedia.org/fgij/fg.htm?mol=5JBQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jbq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5JBQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.006Å</td></tr> |
| - | <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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=H14:(2S,3R)-BETA-HYDROXY-PHENYLALANINE'>H14</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MH6:3-HYDROXY-2-IMINOPROPANOIC+ACID'>MH6</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tufA, b3339, JW3301 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5jbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jbq OCA], [https://pdbe.org/5jbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jbq RCSB], [https://www.ebi.ac.uk/pdbsum/5jbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jbq ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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] | + | [https://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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Palestrant, D]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Stams, T]] | + | [[Category: Palestrant D]] |
| - | [[Category: Elongation factor]] | + | [[Category: Stams T]] |
| - | [[Category: Natural product inhibitor]]
| + | |
| - | [[Category: Rna binding protein-antimicrobial complex]]
| + | |
| Structural highlights
5jbq is a 2 chain structure with sequence from Escherichia coli K-12 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.006Å |
| Ligands: | , , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
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]
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. Antibacterial and Solubility Optimization of Thiomuracin A. J Med Chem. 2016 Jul 12. PMID:27355833 doi:http://dx.doi.org/10.1021/acs.jmedchem.6b00726
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