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Cold active .beta.-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9 Ă resolution
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SYSNO ASEP 0021388 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title Cold active .beta.-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9 Ă resolution Title Chladově aktivní .beta.-galaktosidasa z bakterie Arthrobacter sp. C2-2 tvoří kompaktní 660 kDa hexamery; krystalová struktura s rozlišením 1.9 Ă Author(s) Skálová, Tereza (UMCH-V) RID
Dohnálek, Jan (UMCH-V) RID
Spiwok, V. (CZ)
Lipovová, P. (CZ)
Vondráčková, Eva (UMCH-V)
Petroková, Hana (UMCH-V)
Dušková, Jarmila (UMCH-V) RID
Strnad, Hynek (UMG-J) RID
Králová, B. (CZ)
Hašek, Jindřich (UMCH-V) RIDSource Title Journal of Molecular Biology. - : Elsevier - ISSN 0022-2836
Roč. 353, č. 2 (2005), s. 282-294Number of pages 13 s. Language eng - English Country GB - United Kingdom Keywords glycosyl hydrolase ; .beta.-galactosidase ; cold-active Subject RIV EB - Genetics ; Molecular Biology R&D Projects GA204/02/0843 GA ČR - Czech Science Foundation (CSF) KJB500500512 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z40500505 - UMCH-V (2005-2011) DOI 10.1016/j.jmb.2005.08.028 Annotation The X-ray structure of cold-active .beta.-galactosidase (isoenzyme C-2-2-1) from an Antarctic bacterium Arthrobacter sp. C2-2 was solved at 1.9 Ă resolution. The enzyme forms 660 kDa hexamers with active sites opened to the central cavity of the hexamer and connected by eight channels with exterior solvent. To our best knowledge this is the first cold-active .beta.-galactosidase with known structure and also the first known .beta.-galactosidase structure in the form of compact hexamers. The hexamer organization regulates access of substrates and ligands to six active sites and this unique packing present also in solution raises questions about its purpose and function. Workplace Institute of Macromolecular Chemistry Contact Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Year of Publishing 2006
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