4J72

Crystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase

4J72 の概要

• エントリーDOI: 10.2210/pdb4j72/pdb
• 分子名称: Phospho-N-acetylmuramoyl-pentapeptide-transferase, NICKEL (II) ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: alpha-helical membrane protein, membrane enzyme, magnesium binding, undecaprenyl phosphate binding, udp-murnac-pentapeptide binding, membrane, transferase
• 由来する生物種: Aquifex aeolicus
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein (By similarity): O66465
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82075.36

構造登録者

Lee, S.Y.,Chung, B.C.,Gillespie, R.A.,Kwon, D.Y.,Guan, Z.,Zhou, P.,Hong, J. (登録日: 2013-02-12, 公開日: 2013-09-11, 最終更新日: 2024-02-28)

主引用文献

Chung, B.C.,Zhao, J.,Gillespie, R.A.,Kwon, D.Y.,Guan, Z.,Hong, J.,Zhou, P.,Lee, S.Y.
Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.
Science, 341:1012-1016, 2013

PubMed Abstract: MraY (phospho-MurNAc-pentapeptide translocase) is an integral membrane enzyme that catalyzes an essential step of bacterial cell wall biosynthesis: the transfer of the peptidoglycan precursor phospho-MurNAc-pentapeptide to the lipid carrier undecaprenyl phosphate. MraY has long been considered a promising target for the development of antibiotics, but the lack of a structure has hindered mechanistic understanding of this critical enzyme and the enzyme superfamily in general. The superfamily includes enzymes involved in bacterial lipopolysaccharide/teichoic acid formation and eukaryotic N-linked glycosylation, modifications that are central in many biological processes. We present the crystal structure of MraY from Aquifex aeolicus (MraYAA) at 3.3 Å resolution, which allows us to visualize the overall architecture, locate Mg(2+) within the active site, and provide a structural basis of catalysis for this class of enzyme.

PubMed: 23990562
DOI: 10.1126/science.1236501

実験手法

X-RAY DIFFRACTION (3.3 Å)