8RLL

Structure of the apo form of PIB-1 in an Orthorombic space group

8RLL の概要

• エントリーDOI: 10.2210/pdb8rll/pdb
• 分子名称: Class C beta-lactamase-related serine hydrolase (2 entities in total)
• 機能のキーワード: beta-lactamase, ampc, pib-1, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 174279.55

構造登録者

Medrano, F.J.,Romero, A. (登録日: 2024-01-03, 公開日: 2024-08-14, 最終更新日: 2024-09-18)

主引用文献

Medrano, F.J.,Hernando-Amado, S.,Martinez, J.L.,Romero, A.
A new type of Class C beta-lactamases defined by PIB-1. A metal-dependent carbapenem-hydrolyzing beta-lactamase, from Pseudomonas aeruginosa: Structural and functional analysis.
Int.J.Biol.Macromol., 277:134298-134298, 2024

PubMed Abstract: Antibiotic resistance is one of most important health concerns nowadays, and β-lactamases are the most important resistance determinants. These enzymes, based on their structural and functional characteristics, are grouped in four categories (A, B, C and D). We have solved the structure of PIB-1, a Pseudomonas aeruginosa chromosomally-encoded β-lactamase, in its apo form and in complex with meropenem and zinc. These crystal structures show that it belongs to the Class C β-lactamase group, although it shows notable differences, especially in the Ω- and P2-loops, which are important for the enzymatic activity. Functional analysis showed that PIB-1 is able to degrade carbapenems but not cephalosporins, the typical substrate of Class C β-lactamases, and that its catalytic activity increases in the presence of metal ions, especially zinc. They do not bind to the active-site but they induce the formation of trimers that show an increased capacity for the degradation of the antibiotics, suggesting that this oligomer is more active than the other oligomeric species. While PIB-1 is structurally a Class C β-lactamase, the low sequence conservation, substrate profile and its metal-dependence, prompts us to position this enzyme as the founder of a new group inside the Class C β-lactamases. Consequently, its diversity might be wider than expected.

PubMed: 39097051
DOI: 10.1016/j.ijbiomac.2024.134298

実験手法

X-RAY DIFFRACTION (2.72 Å)