1GG4

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

1GG4 の概要

• エントリーDOI: 10.2210/pdb1gg4/pdb
• 分子名称: UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2,6-DIAMINOPIMELATE-D-ALANYL-D-ALANYL LIGASE (2 entities in total)
• 機能のキーワード: alpha/beta sheet, ligase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P11880
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95821.86

構造登録者

Yan, Y.,Munshi, S.,Chen, Z. (登録日: 2000-07-12, 公開日: 2000-12-20, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)