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Crystal structure of the reactive intermediate/imine deaminase A homolog from the Antarctic bacterium Psychrobacter sp. PAMC 21119

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Cited 1 time in scopus
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Title
Crystal structure of the reactive intermediate/imine deaminase A homolog from the Antarctic bacterium Psychrobacter sp. PAMC 21119
Other Titles
남극 호냉성 박테리아 (Psychrobacter sp. PAMC 21119) 유래 deaminase 효소 (Pp-RidA) 의 구조 연구
Authors
Kwon, Sunghark
Lee, Chang Woo
Koh, Hye Yeon
Park, Hyun
Lee, Jun Hyuck
Park, Hyun Ho
Subject
Biochemistry & Molecular Biology; Biophysics
Keywords
Antarctic bacterium; Cold-adaptability; Deamination; Psychrophile; RidA
Issue Date
2020-02
Citation
Sunghark Kwon, et al. 2020. "Crystal structure of the reactive intermediate/imine deaminase A homolog from the Antarctic bacterium Psychrobacter sp. PAMC 21119". BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 522(3): 585-591.
Abstract
The RidA subfamily proteins catalyze the deamination reaction of enamine/imine intermediates, which are metabolites of amino acids such as threonine and serine. Numerous structural and functional studies have been conducted on RidA isolated from mesophiles and thermophiles. However, little is known about the structure of the RidA proteins isolated from psychrophiles. In the present study, we elucidated the crystal structure of RidA from the Antarctic bacterium Psychrobacter sp. PAMC 21119 (Pp-RidA) at 1.6 A resolution to identify the structural properties contributing to cold-adaptability. Although the overall structure of Pp-RidA is similar to those of its homologues, it exhibits specific structural arrangements of a loop positioned near the active site, which is assumed to play a role in covering the active site of catalysis. In addition, the surface electrostatic potential of Pp-RidA suggested that it exhibits stronger electrostatic distribution relative to its homologues. Our results provide novel insights into the key determinants of cold-adaptability.
URI
https://repository.kopri.re.kr/handle/201206/10495
DOI
http://dx.doi.org/10.1016/j.bbrc.2019.11.139
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