1gg4
From Proteopedia
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CRYSTAL STRUCTURE OF ESCHERICHIA COLI UDPMURNAC-TRIPEPTIDE D-ALANYL-D-ALANINE-ADDING ENZYME (MURF) AT 2.3 ANGSTROM RESOLUTION
Overview
MurF is required to catalyze the final step in the synthesis of the, cytoplasmic precursor of the bacterial cell wall peptidoglycan, rendering, it an attractive target for antibacterial drug development. The crystal, structure of the MurF apo-enzyme has been determined using the, multiwavelength anomalous dispersion method and refined to 2.3 A, resolution. It contains three consecutive open alpha/beta-sheet domains., In comparison with the complex crystal structures of MurD and its, substrates, The topology of the N-terminal domain of MurF is unique, while, its central and C-terminal domains exhibit similar mononucleotide and, dinucleotide-binding folds, respectively. The apo-enzyme of MurF crystal, structure reveals an open conformation with the three domains juxtaposed, in a crescent-like arrangement creating a wide-open space where substrates, are expected to bind. As such, catalysis is not feasible and significant, domain closure is expected upon substrate binding.
About this Structure
1GG4 is a Single protein structure of sequence from Escherichia coli. Active as Deleted entry, with EC number 6.3.2.15 Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli UDPMurNAc-tripeptide d-alanyl-d-alanine-adding enzyme (MurF) at 2.3 A resolution., Yan Y, Munshi S, Leiting B, Anderson MS, Chrzas J, Chen Z, J Mol Biol. 2000 Dec 1;304(3):435-45. PMID:11090285
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