The Crystal Structure of a
Streptomyces thermoviolaceus
TIM-barrel
X-ray crystallography
chitinase
glycoside hydrolase
structure and function relationship
thermostability
α+β-domain
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
21 Apr 2020
21 Apr 2020
Historique:
received:
02
04
2020
revised:
17
04
2020
accepted:
19
04
2020
entrez:
25
4
2020
pubmed:
25
4
2020
medline:
26
1
2021
Statut:
epublish
Résumé
Analyzing the structure of proteins from extremophiles is a promising way to study the rules governing the protein structure, because such proteins are results of structural and functional optimization under well-defined conditions. Studying the structure of chitinases addresses an interesting aspect of enzymology, because chitin, while being the world's second most abundant biopolymer, is also a recalcitrant substrate. The crystal structure of a thermostable chitinase from
Identifiants
pubmed: 32326166
pii: ijms21082892
doi: 10.3390/ijms21082892
pmc: PMC7215727
pii:
doi:
Substances chimiques
Disulfides
0
Chitinases
EC 3.2.1.14
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Narodowe Centrum Nauki
ID : UMO-2017/27/B/NZ1/02201
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