1h3g

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1h3g, resolution 2.1Å

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CYCLOMALTODEXTRINASE FROM FLAVOBACTERIUM SP. NO. 92: FROM DNA SEQUENCE TO PROTEIN STRUCTURE

Overview

Starting with oligopeptide sequences and using PCR, the gene of the, cyclodextrinase from Flavobacterium sp. no. 92 was derived from the, genomic DNA. The gene was sequenced and expressed in Escherichia coli; the, gene product was purified and crystallized. An X-ray diffraction analysis, using seleno-methionines with multiwavelength anomalous diffraction, techniques yielded the refined 3D structure at 2.1 A resolution. The, enzyme hydrolyzes alpha(1,4)-glycosidic bonds of cyclodextrins and linear, malto-oligosaccharides. It belongs to the glycosylhydrolase family no. 13, and has a chain fold similar to that of alpha-amylases, cyclodextrin, glycosyltransferases, and other cyclodextrinases. In contrast with most, family members but in agreement with other cyclodextrinases, the enzyme, ... [(full description)]

About this Structure

1H3G is a [Single protein] structure of sequence from [Flavobacterium sp. 92] with CA as [ligand]. Active as [[1]], with EC number [3.2.1.54]. Full crystallographic information is available from [OCA].

Reference

Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92., Fritzsche HB, Schwede T, Schulz GE, Eur J Biochem. 2003 May;270(10):2332-41. PMID:12752453

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