1cdg
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(New page: 200px<br /><applet load="1cdg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cdg, resolution 2.0Å" /> '''NUCLEOTIDE SEQUENCE A...)
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Revision as of 10:14, 20 November 2007
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NUCLEOTIDE SEQUENCE AND X-RAY STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE FROM BACILLUS CIRCULANS STRAIN 251 IN A MALTOSE-DEPENDENT CRYSTAL FORM
Overview
The cyclodextrin glycosyltransferase (CGTase, EC 2.4.1.19) gene from, Bacillus circulans strain 251 was cloned and sequenced. It was found to, code for a mature protein of 686 amino acid residues, showing 75% identity, to the CGTase from B. circulans strain 8. The X-ray structure of the, CGTase was elucidated in a maltodextrin-dependent crystal form and refined, against X-ray diffraction data to 2.0 A resolution. The structure of the, enzyme is nearly identical to the CGTase from B. circulans strain 8. Three, maltose binding sites are observed at the protein surface, two in domain E, and one in domain C. The maltose-dependence of CGTase crystallization can, be ascribed to the proximity of two of the maltose binding sites to, intermolecular crystal contacts. The maltose molecules bound in the E, domain interact with several residues implicated in a raw starch binding, motif conserved among a diverse group of starch converting enzymes.
About this Structure
1CDG is a Single protein structure of sequence from Bacillus circulans with MAL and CA as ligands. Active as Cyclomaltodextrin glucanotransferase, with EC number 2.4.1.19 Full crystallographic information is available from OCA.
Reference
Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form., Lawson CL, van Montfort R, Strokopytov B, Rozeboom HJ, Kalk KH, de Vries GE, Penninga D, Dijkhuizen L, Dijkstra BW, J Mol Biol. 1994 Feb 18;236(2):590-600. PMID:8107143
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