Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form

Catherine L. Lawson, Rob van Montfort, Boris Strokopytov, Henriëtte J. Rozeboom, Kor H. Kalk, Gert E. de Vries, Dirk Penninga, Lubbert Dijkhuizen, Bauke W. Dijkstra

Research output: Contribution to journalArticlepeer-review

213 Scopus citations

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 Å 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 O. 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.

Original languageEnglish (US)
Pages (from-to)590-600
Number of pages11
JournalJournal of molecular biology
Volume236
Issue number2
DOIs
StatePublished - Feb 17 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Keywords

  • Bacillus circulans
  • Crystal structure
  • Cyclodextrin glycosyltransferase
  • Nucleotide sequence
  • Starch binding

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