Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
 
 
DownloadE-Mail
 Lokale TagsFreigabegeschichteDetailsÜbersicht
  Description of Transport Tunnel in Haloalkane Dehalogenase Variant LinB D147C+L177C from Sphingobium japonicum

Iermak, I., Degtjarik, O., Havlickova, P., Kuty, M., Chaloupkova, R., Damborsky, J., et al. (2021). Description of Transport Tunnel in Haloalkane Dehalogenase Variant LinB D147C+L177C from Sphingobium japonicum. Catalysts, 11(1): 5. doi:10.3390/catal11010005.

Item is

 

einblenden: alle ausblenden: alle

Basisdaten

einblenden: ausblenden:
Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0007-F1AA-9 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0007-F1AB-8
Genre: Zeitschriftenartikel

Dateien

einblenden: Dateien
ausblenden: Dateien
:
catalysts-11-00005-v2.pdf (Verlagsversion), 11MB
Öffnen   Speichern
Datei-Permalink:
https://hdl.handle.net/21.11116/0000-0007-F1AC-7
Name:
catalysts-11-00005-v2.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Öffnen
Copyright Datum:
-
Copyright Info:
© 2020 by the authors.
Lizenz:
https://creativecommons.org/licenses/by/4.0/

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Iermak, Iuliia1, Autor
Degtjarik, Oksana1, Autor
Havlickova, Petra1, Autor
Kuty, Michal1, Autor
Chaloupkova, Radka1, Autor
Damborsky, Jiri1, Autor
Prudnikova, Tatyana1, Autor
Kuta Smatanova, Ivana1, Autor
Affiliations:
1external, ou_persistent22              

Inhalt

einblenden:
ausblenden:
Schlagwörter: Chemistry; bacterial enzyme; haloalkane dehalogenase; mutant form; crystallization; tertiary structure; disulfide bond; protein engineering; molecular dynamics; access tunnel; substrate specificity;
 Zusammenfassung: The activity of enzymes with active sites buried inside their protein core highly depends on the efficient transport of substrates and products between the active site and the bulk solvent. The engineering of access tunnels in order to increase or decrease catalytic activity and specificity in a rational way is a challenging task. Here, we describe a combined experimental and computational approach to characterize the structural basis of altered activity in the haloalkane dehalogenase LinB D147C+L177C variant. While the overall protein fold is similar to the wild type enzyme and the other LinB variants, the access tunnels have been altered by introduced cysteines that were expected to form a disulfide bond. Surprisingly, the mutations have allowed several conformations of the amino acid chain in their vicinity, interfering with the structural analysis of the mutant by X-ray crystallography. The duration required for the growing of protein crystals changed from days to 1.5 years by introducing the substitutions. The haloalkane dehalogenase LinB D147C+L177C variant crystal structure was solved to 1.15 angstrom resolution, characterized and deposited to Protein Data Bank under PDB ID 6s06.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2021
 Publikationsstatus: Online veröffentlicht
 Seiten: 15
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000609997300001
DOI: 10.3390/catal11010005
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Catalysts
  Kurztitel : Catalysts
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Basel : MDPI
Seiten: - Band / Heft: 11 (1) Artikelnummer: 5 Start- / Endseite: - Identifikator: ISSN: 2073-4344
CoNE: https://pure.mpg.de/cone/journals/resource/2073-4344