Crystal structure of the reactive intermediate/imine deaminase A homolog from the Antarctic bacterium Psychrobacter sp. PAMC 21119.
Antarctic bacterium
Cold-adaptability
Deamination
Psychrophile
RidA
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
12 02 2020
12 02 2020
Historique:
received:
12
11
2019
accepted:
20
11
2019
pubmed:
2
12
2019
medline:
1
9
2020
entrez:
2
12
2019
Statut:
ppublish
Résumé
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 Å 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.
Identifiants
pubmed: 31785813
pii: S0006-291X(19)32267-3
doi: 10.1016/j.bbrc.2019.11.139
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Imines
0
Aminohydrolases
EC 3.5.4.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
585-591Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.