1J3G

Solution structure of Citrobacter Freundii AmpD

「1IYA」から置き換えられました 「1J2S」から置き換えられました

1J3G の概要

• エントリーDOI: 10.2210/pdb1j3g/pdb
• 分子名称: AmpD protein, ZINC ION (2 entities in total)
• 機能のキーワード: mixed alpha-beta, hydrolase
• 由来する生物種: Citrobacter freundii
• 細胞内の位置: Cytoplasm (By similarity): P82974
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20936.77

構造登録者

Liepinsh, E.,Genereux, C.,Dehareng, D.,Joris, B.,Otting, G. (登録日: 2003-01-31, 公開日: 2003-02-18, 最終更新日: 2023-12-27)

主引用文献

Liepinsh, E.,Genereux, C.,Dehareng, D.,Joris, B.,Otting, G.
NMR Structure of Citrobacter freundii AmpD, Comparison with Bacteriophage T7 Lysozyme and Homology with PGRP Domains
J.Mol.Biol., 327:833-842, 2003

PubMed Abstract: AmpD is a bacterial amidase involved in the recycling of cell-wall fragments in Gram-negative bacteria. Inactivation of AmpD leads to derepression of beta-lactamase expression, presenting a major pathway for the acquisition of constitutive antibiotic resistance. Here, we report the NMR structure of AmpD from Citrobacter freundii (PDB accession code 1J3G). A deep substrate-binding pocket explains the observed specificity for low molecular mass substrates. The fold is related to that of bacteriophage T7 lysozyme. Both proteins bind zinc at a conserved site and require zinc for amidase activity, although the enzymatic mechanism seems to differ in detail. The structure-based sequence alignment identifies conserved features that are also conserved in the eukaryotic peptidoglycan recognition protein (PGRP) domains, including the zinc-coordination site in several of them. PGRP domains thus belong to the same fold family and, where zinc-binding residues are conserved, may have amidase activity. This hypothesis is supported by the observation that human serum N-acetylmuramyl-L-alanine amidase seems to be identical with a soluble form of human PGRP-L.

PubMed: 12654266
DOI: 10.1016/S0022-2836(03)00185-2

実験手法

SOLUTION NMR