1gow

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File:1gow.gif


1gow, resolution 2.6Å

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BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS

OverviewOverview

Enzymes from hyperthermophilic organisms must operate at temperatures, which rapidly denature proteins from mesophiles. The structural basis of, this thermostability is still poorly understood. Towards a further, understanding of hyperthermostability, we have determined the crystal, structure of the beta-glycosidase (clan GH-1A, family 1) from the, hyperthermophilic archaeon Sulfolobus solfataricus at 2.6 A resolution., The enzyme is a tetramer with subunit molecular mass at 60 kDa, and, crystallises with half of the tetramer in the asymmetric unit. The, structure is a (betaalpha)8 barrel, but with substantial elaborations, between the beta-strands and alpha-helices in each repeat. The active site, occurs at the centre of the top face of the barrel and is connected to the, surface by a ... [(full description)]

About this StructureAbout this Structure

1GOW is a [Single protein] structure of sequence from [Sulfolobus solfataricus]. Active as [Beta-galactosidase], with EC number [3.2.1.23]. Structure known Active Sites: CTA and CTB. Full crystallographic information is available from [OCA].

ReferenceReference

Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability., Aguilar CF, Sanderson I, Moracci M, Ciaramella M, Nucci R, Rossi M, Pearl LH, J Mol Biol. 1997 Sep 5;271(5):789-802. PMID:9299327

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