Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin

Proteins: Structure, Function and Genetics

Volumn 71, Issue 2, 2008, Pages 1032-1037

  Yoon, Hye Jin ^a   Sang, Jae Lee ^a   Mikami, Bunzo ^b   Park, Hyun Ju ^c   Yoo, Jakyung ^c   Se, Won Suh ^a  

^a Seoul National University   (South Korea)

^b KYOTO UNIVERSITY   (Japan)

^c Sungkyunkwan University   (South Korea)

Author keywords

Antibacterial target; Fosfomycin; MurA; MurZ; UDP N acetylglucosamine enolpyruvyl transferase

Indexed keywords

BACTERIAL ENZYME; FOSFOMYCIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; HAEMOPHILUS INFLUENZAE; PRIORITY JOURNAL;

ALKYL AND ARYL TRANSFERASES; AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; FOSFOMYCIN; HAEMOPHILUS INFLUENZAE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; URIDINE DIPHOSPHATE N-ACETYLGLUCOSAMINE;

HAEMOPHILUS INFLUENZAE;

EID: 41149117918     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21959     Document Type: Article

References (16)

1. El Zoeiby A, Sanschagrin F, Levesque RC. Structure and fonction of the Mur enzymes: development of novel inhibitors. Mol Microbiol 2003;47:1-12.
2. Bugg TD, Walsh CT. Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: enzymology, antibiotics, and antibiotic resistance. Nat Prod Rep 1992;9:199-215.
3. 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;177:4194-4197.
4. Du WS, Brown JR, Sylvester DR, Huang JZ, Chalker AF, So CY, Holmes DJ, Payne DJ, Wallis NG. Two active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in gram-positive bacteria. J Bacteriol 2000;182:4146-4152.
5. Kahan FM, Kahan JS, Cassidy PJ, Kropp H. The mechanism of action of fosfomycin (phosphonomycin). Ann N Y Acad Sci 1974;235:364-386.
6. Baum EZ, Montenegro DA, Licata L, Turchi I, Webb GC, Foleno BD, Bush K. Identification and characterization of new inhibitors of the Escherichia coli MurA enzyme. Antimicrob Agents Chemother 2001;45:3182-3188.
7. DeVito JA, Mills JA, Liu VG, Agarwal A, Sizemore CF, Yao Z, Stoughton DM, Cappiello MG, Barbosa MD, Foster LA, Pompliano DL. An array of target-specific screening strains for antibacterial discovery. Nat Biotechnol 2002;20:478-483.
8. Molina-López J, Sanschagrin F, Levesque RC. A peptide inhibitor of MurA UDP-N-acetylglucosamine enolpyruvyl transferase: the first committed step in peptidoglycan biosynthesis. Peptides 2006;27:3115-3121.
9. Schönbrunn E, Sack S, Eschenburg S, Perrakis A, Krekel F, Amrhein N, Mandelkow E. Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin. Structure 1996;4:1065-1075.
10. 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;4:1465-1474.
11. Yoon HJ, Ku MJ, Ahn HJ, Lee BI, Mikami B, Suh SW. Crystallization and preliminary X-ray crystallographic analysis of UDP-N-Acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-Acetylglucosamine and fosfomycin. Mol Cells 2005;19:398-401.
12. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr Sect D Biol Crystallogr 1998;54:905-921.
13. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr Sect A 1991;47:110-119.
14. Skarzynski T, Kim DH, Lees WJ, Walsh CT, Duncan K. Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA. Biochemistry 1998;37:2572-2577.
15. Eschenburg S, Priestman M, Schonbrunn E. Evidence that the fosfomycin target Cys(115) in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release. J Biol Chem 2005;280:3757-3763.
16. Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL