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Comparative X-ray analysis of the un-liganded fosfomycin-target murA
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title
Comparative X-ray analysis of the un-liganded fosfomycin-target murA
(English)
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author name string
S Eschenburg
series ordinal
1
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E Schönbrunn
series ordinal
2
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language of work or name
English
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publication date
1 August 2000
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published in
Proteins
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volume
40
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issue
2
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page(s)
290-8
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The mechanism of action of fosfomycin (phosphonomycin)
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Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin
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Studies on the conformational changes in the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine enolpyruvyltransferase (MurA).
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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
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Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA
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The UDP-N-acetylglucosamine 1-carboxyvinyl-transferase of Enterobacter cloacae. Molecular cloning, sequencing of the gene and overexpression of the enzyme
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Identifiers
DOI
10.1002/(SICI)1097-0134(20000801)40:2<290::AID-PROT90>3.0.CO;2-0
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PubMed publication ID
10842342
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