X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method.

X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method. Research Abstract Details 

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X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method. Abstract Text:

A Takenaka,K Kizawa,T Hata,S Sato,E Misaka,C Tamura,Y Sasada,

The molecular structure of lipoamide dehydrogenase from baker's yeast has been determined at 4.5 A resolution by molecular replacement techniques using the known structure of human erythrocyte glutathione reductase as a starting model. The enzyme crystallizes in the space group P2(1)2(1)2(1) with a = 98.6(2), b = 162.0(2), c = 69.4(2) A. There is one molecule per asymmetric unit. The enzyme is a dimeric protein of identical subunits related by a local two-fold symmetry. Comparison of the tertiary structures between glutathione reductase and the present enzyme shows that the folding is almost the same except for the N and C termini, although some slight shortening or shifting of alpha-helices was found in the electron density map. FAD molecules are found at similar positions to those of glutathione reductase. Since the amino acid residues around FAD and NAD binding sites and at the reaction centers of the two enzymes are strongly conserved, the lipoamide dehydrogenase may catalyze the opposite reaction through a similar mechanism to that proposed for glutathione reductase. The newly found C terminus is located near the edge of a deep cave at the interface between the two subunits. These additional 18 residues form a narrow entrance to the cave, in which the long chain of the dihydrolipoyl moiety of lipoate acetyltransferase will be bound.

X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method. Publishing Authors By Initials

A Takenaka,K Kizawa,T Hata,S Sato,E Misaka,C Tamura,Y Sasada,

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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X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 103

Page Numbers: 463-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Mar

YEAR: 1988

X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method. Information

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LANGUAGE: eng

NlmUniqueID: 376600

X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method. Keywords Mesh Terms:

KEYWORDS: X-Ray Diffraction

MESH TERMS: enzymology

Chemical & Substance for Abstract: X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method. Information

Substance Name: Glutathione Reductase

Registry Number: EC 1.8.1.7

Grant and Affiliation Information for X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method.

AFFILIATION: Faculty of Science, Department of Life Science, Tokyo Institute of Technology, Kanagawa.

Country: JAPAN

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MEDLINETA: J Biochem

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