Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri

Citation
Y. Mezaki et al., Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri, BIOS BIOT B, 65(1), 2001, pp. 222-225
Citations number
17
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Agricultural Chemistry","Biochemistry & Biophysics
Journal title
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
ISSN journal
0916-8451 → ACNP
Volume
65
Issue
1
Year of publication
2001
Pages
222 - 225
Database
ISI
SICI code
0916-8451(200101)65:1<222:CASAOI>2.0.ZU;2-E
Abstract
The intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri (G4- 1), which has a raw starch binding domain, has been crystallized. The struc ture was identified (PDB entry 1GCY) by the molecular replacement method us ing the structure of its catalytic domain (G4-2). The result showed that th e raw starch binding domain is in a disordered state, the corresponding ele ctron densities being almost invisible. Superposition of these two enzyme f orms showed evidence for the possible location of the raw starch binding do main (SBD), This crystal is a novel case, in that it forms a regular lattic e incorporating flexibly bound SBD in the channel of crystal packing of the catalytic domains.