Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis.

Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis. Research Abstract Details 

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Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis. Abstract Text:

H Kizaki,Y Hata,K Watanabe,Y Katsube,Y Suzuki,

The crystal structure of an oligo-1,6-glucosidase from Bacillus cereus ATCC7064 was determined by the X-ray diffraction method at 3.0 A resolution. The structure was solved by the multiple isomorphous replacement method and refined to a crystallographic R-factor of 0.208, using the molecular dynamics refinement program, X-PLOR. The electron density map revealed the folding of a polypeptide chain consisting of 558 amino acid residues. The molecule can be subdivided into three domains (N-terminal domain, subdomain, and C-terminal domain). The N-terminal domain has an (alpha/beta)8-barrel structure called the TIM-barrel structure. The C-terminal domain is characterized by a beta-barrel structure composed of eight antiparallel beta-strands, while the subdomain has a loop-rich structure with a small alpha-helix and a beta-sheet. The enzyme has a large cleft between the N-terminal domain and the subdomain. The cleft leads from the molecular surface to the molecular center. The bottom of the cleft is at the C-terminal end of the parallel beta-strands of the (alpha/beta)8-barrel. These structural features closely resemble those of alpha-amylases from Aspergillus oryzae and pig pancreas.

Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis. Publishing Authors By Initials

H Kizaki,Y Hata,K Watanabe,Y Katsube,Y Suzuki,

For similar investigative techniques: chemistry, analytical: crystallography: x-ray diffraction research abstracts see: investigative techniques: chemistry, analytical: crystallography: x-ray diffraction research

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Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 113

Page Numbers: 646-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jun

YEAR: 1993

Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis. Keywords Mesh Terms:

KEYWORDS: X-Ray Diffraction

MESH TERMS: chemistry

Chemical & Substance for Abstract: Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis. Information

Substance Name: Oligo-1,6-Glucosidase

Registry Number: EC 3.2.1.10

Grant and Affiliation Information for Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis.

AFFILIATION: Department of Agricultural Chemistry, Kyoto Prefectural University.

Country: JAPAN

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MEDLINETA: J Biochem

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