Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F19%3A43899251" target="_blank" >RIV/60076658:12310/19:43899251 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/19:00505903 RIV/68378050:_____/19:00505903 RIV/61388963:_____/19:00505284 RIV/00216224:14310/19:00108194 RIV/00159816:_____/19:00071077
Result on the web
<a href="https://scripts.iucr.org/cgi-bin/paper?cnor=no5154&buy=yes#buy" target="_blank" >https://scripts.iucr.org/cgi-bin/paper?cnor=no5154&buy=yes#buy</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S2053230X19002796" target="_blank" >10.1107/S2053230X19002796</a>
Alternative languages
Result language
angličtina
Original language name
Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5
Original language description
Haloalkane dehalogenases (HLDs) convert halogenated aliphatic pollutants to less toxic compounds by a hydrolytic mechanism. Owing to their broad substrate specificity and high enantioselectivity, haloalkane dehalogenases can function as biosensors to detect toxic compounds in the environment or can be used for the production of optically pure compounds. Here, the structural analysis of the haloalkane dehalogenase DpcA isolated from the psychrophilic bacterium Psychrobacter cryohalolentis K5 is presented at the atomic resolution of 1.05 angstrom. This enzyme exhibits a low temperature optimum, making it attractive for environmental applications such as biosensing at the subsurface environment, where the temperature typically does not exceed 25 degrees C. The structure revealed that DpcA possesses the shortest access tunnel and one of the most widely open main tunnels among structural homologs of the HLD-I subfamily. Comparative analysis revealed major differences in the region of the alpha 4 helix of the cap domain, which is one of the key determinants of the anatomy of the tunnels. The crystal structure of DpcA will contribute to better understanding of the structure-function relationships of cold-adapted enzymes.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section F-Structural Biology and Communications
ISSN
2053-230X
e-ISSN
—
Volume of the periodical
75
Issue of the periodical within the volume
MAY 2019
Country of publishing house
GB - UNITED KINGDOM
Number of pages
8
Pages from-to
324-331
UT code for WoS article
000466795900002
EID of the result in the Scopus database
2-s2.0-85065171699