6ET6

Crystal structure of muramidase from Acinetobacter baumannii AB 5075UW prophage

6ET6 の概要

• エントリーDOI: 10.2210/pdb6et6/pdb
• 分子名称: Lysozyme, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: muramidase, lysozyme, acinetobacter baumannii, antimicrobial protein
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21818.56

構造登録者

Boyko, K.M.,Nikolaeva, A.Y.,Sykilinda, N.N.,Shneider, M.M.,Miroshnikov, K.A.,Popov, V.O. (登録日: 2017-10-25, 公開日: 2018-09-05, 最終更新日: 2024-01-17)

主引用文献

Sykilinda, N.N.,Nikolaeva, A.Y.,Shneider, M.M.,Mishkin, D.V.,Patutin, A.A.,Popov, V.O.,Boyko, K.M.,Klyachko, N.L.,Miroshnikov, K.A.
Structure of anAcinetobacterBroad-Range Prophage Endolysin Reveals a C-Terminal alpha-Helix with the Proposed Role in Activity against Live Bacterial Cells.
Viruses, 10:-, 2018

PubMed Abstract: Proteins that include enzymatic domain degrading the bacterial cell wall and a domain providing transport through the bacterial outer membrane are considered as prospective compounds to combat pathogenic Gram-negative bacteria. This paper presents an isolation and study of an enzyme of this class naturally encoded in the prophage region of AB 5075 genome. Recombinant protein expressed in exhibits an antimicrobial activity with respect to live cultures of Gram-negative bacteria reducing the population of viable bacteria by 1.5⁻2 log colony forming units (CFU)/mL. However the protein becomes rapidly inactivated and enables the bacteria to restore the population. AcLys structure determined by X-ray crystallography reveals a predominantly α—helical fold similar to bacteriophage P22 lysozyme. The С-terminal part of AcLys polypeptide chains forms an α—helix enriched by Lys and Arg residues exposed outside of the protein globule. Presumably this type of structure of the C-terminal α—helix has evolved evolutionally enabling the endolysin to pass the inner membrane during the host lysis or, potentially, to penetrate the outer membrane of the Gram-negative bacteria.

PubMed: 29882827
DOI: 10.3390/v10060309

実験手法

X-RAY DIFFRACTION (1.2 Å)