6ET6

Crystal structure of muramidase from Acinetobacter baumannii AB 5075UW prophage

Summary for 6ET6

• Entry DOI: 10.2210/pdb6et6/pdb
• Descriptor: Lysozyme, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: muramidase, lysozyme, acinetobacter baumannii, antimicrobial protein
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 1
• Total formula weight: 21818.56

Authors

Boyko, K.M.,Nikolaeva, A.Y.,Sykilinda, N.N.,Shneider, M.M.,Miroshnikov, K.A.,Popov, V.O. (deposition date: 2017-10-25, release date: 2018-09-05, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.2 Å)