1GG4

CRYSTAL STRUCTURE OF ESCHERICHIA COLI UDPMURNAC-TRIPEPTIDE D-ALANYL-D-ALANINE-ADDING ENZYME (MURF) AT 2.3 ANGSTROM RESOLUTION

Summary for 1GG4

• Entry DOI: 10.2210/pdb1gg4/pdb
• Descriptor: UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2,6-DIAMINOPIMELATE-D-ALANYL-D-ALANYL LIGASE (2 entities in total)
• Functional Keywords: alpha/beta sheet, ligase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P11880
• Total number of polymer chains: 2
• Total formula weight: 95821.86

Authors

Yan, Y.,Munshi, S.,Chen, Z. (deposition date: 2000-07-12, release date: 2000-12-20, Last modification date: 2024-10-09)

Primary citation

Yan, Y.,Munshi, S.,Leiting, B.,Anderson, M.S.,Chrzas, J.,Chen, Z.
Crystal structure of Escherichia coli UDPMurNAc-tripeptide d-alanyl-d-alanine-adding enzyme (MurF) at 2.3 A resolution.
J.Mol.Biol., 304:435-445, 2000

PubMed Abstract: 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.

PubMed: 11090285
DOI: 10.1006/jmbi.2000.4215

Experimental method

X-RAY DIFFRACTION (2.3 Å)