Structural Properties and Electrostatics of Cold-active beta-Galactosidase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F07%3A00019134" target="_blank" >RIV/60461373:22330/07:00019134 - isvavai.cz</a>
Result on the web
—
DOI - Digital Object Identifier
—
Alternative languages
Result language
angličtina
Original language name
Structural Properties and Electrostatics of Cold-active beta-Galactosidase
Original language description
Arthrobacter sp. C2-2, a soil bacteria found on an island near Antarctica, belongs to psychrotrophic, i.e. cold tolerant, microorganisms. Structure of its betagalactosidase (hydrolase cleaving lactose into galactose and glucose), iso-enzyme C-2-2-1, wassolved up to 1.9 ? resolution. The beta-galactosidase belongs to glycosyl hydrolase structural family 2 and has 30% sequence identity with Escherichia coli beta-galactosidase. In spite of the chain similarity, both enzymes differ in their oligomerizationstates. Escherichia coli beta-galactosidase is known to be active only in the form of tetramers, while the cold-active Arthrobacter sp. C2-2 beta-galactosidase forms compact hexamers with active sites oriented into an internal cavity, connected by threetypes of channels with exterior solvent. Additionally, sequence differences between both enzymes exist in the active site.
Czech name
Strukturní vlastnosti a elektrostatika chladově-aktivní beta-galaktosidasy
Czech description
Strukturní vlastnosti a elektrostatika chladově-aktivní beta-galaktosidasy byla presentována
Classification
Type
D - Article in proceedings
CEP classification
CE - Biochemistry
OECD FORD branch
—
Result continuities
Project
<a href="/en/project/KJB500500512" target="_blank" >KJB500500512: Structural studies of beta-galactosidase from psychrotrophic microorganisms; analysis of biologically and technologically significant complexes</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2007
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Article name in the collection
Acta Crystallogr., Sect.A: Cryst.Phys.,Diffr.,Theor.Gen.Crystallogr.
ISBN
—
ISSN
0567-7394
e-ISSN
—
Number of pages
2
Pages from-to
"s125"-"s126"
Publisher name
IUCr, International Union of Crystallography
Place of publication
Chester
Event location
—
Event date
—
Type of event by nationality
—
UT code for WoS article
—