3LEZ

Crystal structure of a halotolerant bacterial beta-lactamase

3LEZ の概要

• エントリーDOI: 10.2210/pdb3lez/pdb
• 分子名称: Beta-lactamase, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: beta-lactamase, antibiotic resistance, halotolerant, deep-sea bacterium, hydrolase
• 由来する生物種: Oceanobacillus iheyensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29463.00

構造登録者

Smith, C.A.,Vakulenko, S.B. (登録日: 2010-01-15, 公開日: 2010-02-02, 最終更新日: 2024-02-21)

主引用文献

Toth, M.,Smith, C.,Frase, H.,Mobashery, S.,Vakulenko, S.
An antibiotic-resistance enzyme from a deep-sea bacterium
J.Am.Chem.Soc., 132:816-823, 2010

PubMed Abstract: We describe herein a highly proficient class A beta-lactamase OIH-1 from the bacterium Oceanobacillus iheyensis, whose habitat is the sediment at a depth of 1050 m in the Pacific Ocean. The OIH-1 structure was solved by molecular replacement and refined at 1.25 A resolution. OIH-1 has evolved to be an extremely halotolerant beta-lactamase capable of hydrolyzing its substrates in the presence of NaCl at saturating concentration. Not only is this the most highly halotolerant bacterial enzyme structure known to date, it is also the highest resolution halophilic protein structure yet determined. Evolution of OIH-1 in the salinity of the ocean has resulted in a molecular surface that is coated with acidic residues, a marked difference from beta-lactamases of terrestrial sources. OIH-1 is the first example of an antibiotic-resistance enzyme that has evolved in the depths of the ocean in isolation from clinical selection and gives us an extraordinary glimpse into protein evolution under extreme conditions. It represents evidence for the existence of a reservoir of antibiotic-resistance enzymes in nature among microbial populations from deep oceanic sources.

PubMed: 20000704
DOI: 10.1021/ja908850p

実験手法

X-RAY DIFFRACTION (1.25 Å)