1CDG

NUCLEOTIDE SEQUENCE AND X-RAY STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE FROM BACILLUS CIRCULANS STRAIN 251 IN A MALTOSE-DEPENDENT CRYSTAL FORM

Summary for 1CDG

• Entry DOI: 10.2210/pdb1cdg/pdb
• Related PRD ID: PRD_900001
• Descriptor: CYCLODEXTRIN GLYCOSYL-TRANSFERASE, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: transferase(glucanotransferase)
• Biological source: Bacillus circulans
• Total number of polymer chains: 1
• Total formula weight: 75682.53

Authors

Lawson, C.L.,Van Montfort, R.,Strokopytov, B.V.,Kalk, K.H.,Rozeboom, H.J.,Dijkstra, B.W. (deposition date: 1993-08-02, release date: 1994-01-31, Last modification date: 2024-11-13)

Primary citation

Lawson, C.L.,van Montfort, R.,Strokopytov, B.,Rozeboom, H.J.,Kalk, K.H.,de Vries, G.E.,Penninga, D.,Dijkhuizen, L.,Dijkstra, B.W.
Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form.
J.Mol.Biol., 236:590-600, 1994

PubMed Abstract: 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.

PubMed: 8107143
DOI: 10.1006/jmbi.1994.1168

Experimental method

X-RAY DIFFRACTION (2 Å)