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1yq2

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{{STRUCTURE_1yq2| PDB=1yq2 | SCENE= }}
{{STRUCTURE_1yq2| PDB=1yq2 | SCENE= }}
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'''beta-galactosidase from Arthrobacter sp. C2-2 (isoenzyme C2-2-1)'''
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===beta-galactosidase from Arthrobacter sp. C2-2 (isoenzyme C2-2-1)===
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==Overview==
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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 1.9A 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. This enzyme belongs to glycosyl hydrolase family 2, similarly to Escherichia coli beta-galactosidase, forming tetramers necessary for its enzymatic function. However, we discovered significant differences between these two enzymes affecting the ability of tetramer/hexamer formation and complementation of the active site. This structure reveals new insights into the cold-adaptation mechanisms of enzymatic pathways of extremophiles.
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(as it appears on PubMed at http://www.pubmed.gov), where 16171818 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16171818}}
==About this Structure==
==About this Structure==
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[[Category: Hexamer]]
[[Category: Hexamer]]
[[Category: Tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Jul 5 16:21:40 2008''

Revision as of 13:21, 5 July 2008

Image:1yq2.png

Template:STRUCTURE 1yq2

beta-galactosidase from Arthrobacter sp. C2-2 (isoenzyme C2-2-1)

Template:ABSTRACT PUBMED 16171818

About this Structure

1YQ2 is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.

Reference

Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution., Skalova T, Dohnalek J, Spiwok V, Lipovova P, Vondrackova E, Petrokova H, Duskova J, Strnad H, Kralova B, Hasek J, J Mol Biol. 2005 Oct 21;353(2):282-94. PMID:16171818

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