Literature DB >> 11272837

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

Y Mezaki1, Y Katsuya, M Kubota, Y Matsuura.   

Abstract

The intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri (G4-1), which has a raw starch binding domain, has been crystallized. The structure was identified (PDB entry 1GCY) by the molecular replacement method using the structure of its catalytic domain (G4-2). The result showed that the raw starch binding domain is in a disordered state, the corresponding electron densities being almost invisible. Superposition of these two enzyme forms showed evidence for the possible location of the raw starch binding domain (SBD). This crystal is a novel case, in that it forms a regular lattice incorporating flexibly bound SBD in the channel of crystal packing of the catalytic domains.

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Year:  2001        PMID: 11272837     DOI: 10.1271/bbb.65.222

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  1 in total

1.  Thermostability enhancement and change in starch hydrolysis profile of the maltohexaose-forming amylase of Bacillus stearothermophilus US100 strain.

Authors:  Mamdouh Ben Ali; Bassem Khemakhem; Xavier Robert; Richard Haser; Samir Bejar
Journal:  Biochem J       Date:  2006-02-15       Impact factor: 3.857

  1 in total

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