Enoylpyruvate transferase
From Proteopedia
(Difference between revisions)
| Line 27: | Line 27: | ||
**[[3r38]] – MurA – ''Listeria monocytogenes''<br /> | **[[3r38]] – MurA – ''Listeria monocytogenes''<br /> | ||
**[[3sg1]] – MurA – ''Bacillus anthracis''<br /> | **[[3sg1]] – MurA – ''Bacillus anthracis''<br /> | ||
| + | **[[5ujs]] – MurA – ''Campylobacter jejuni''<BR /> | ||
*MurA binary complex | *MurA binary complex | ||
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**[[3swq]] – EncMurA (mutant) + enoylpyruvyl-UNAG <BR /> | **[[3swq]] – EncMurA (mutant) + enoylpyruvyl-UNAG <BR /> | ||
**[[3v4t]], [[1ryw]] – EncMurA (mutant) + UNAG <BR /> | **[[3v4t]], [[1ryw]] – EncMurA (mutant) + UNAG <BR /> | ||
| + | **[[5u4h]] – MurA + phosphonooxy propanoate – ''Acinetobacter baumannii''<BR /> | ||
| + | **[[5bq2]] – MurA + enoylpyruvyl-UNAG – ''Pseudomonas aeruginosa''<BR /> | ||
*MurA ternary complex with antibiotics | *MurA ternary complex with antibiotics | ||
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**[[3lth]] – EncMurA + UNAG + fosfomycin<BR /> | **[[3lth]] – EncMurA + UNAG + fosfomycin<BR /> | ||
**[[3vcy]] – MurA + UNAG + fosfomycin – ''Vibrio fischeri''<BR /> | **[[3vcy]] – MurA + UNAG + fosfomycin – ''Vibrio fischeri''<BR /> | ||
| + | **[[4r7u]] – MurA + UNAG + fosfomycin – ''Vibrio cholerae''<BR /> | ||
**[[2rl2]] – HiMurA + UNAG + fosfomycin<BR /> | **[[2rl2]] – HiMurA + UNAG + fosfomycin<BR /> | ||
**[[2z2c]] – EcMurA + UNAG + cnicin<BR /> | **[[2z2c]] – EcMurA + UNAG + cnicin<BR /> | ||
Revision as of 08:56, 1 May 2017
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3D Structures of enoylpyruvate transferase
Updated on 01-May-2017
References
- ↑ Brown ED, Vivas EI, Walsh CT, Kolter R. MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli. J Bacteriol. 1995 Jul;177(14):4194-7. PMID:7608103
- ↑ Skarzynski T, Mistry A, Wonacott A, Hutchinson SE, Kelly VA, Duncan K. Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Structure. 1996 Dec 15;4(12):1465-74. PMID:8994972
