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X-ray structure of ...
X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli.
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- Johansson, Tomas (author)
- Chalmers tekniska högskola,Chalmers University of Technology,Köpenhamns universitet,University of Copenhagen
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- Oswald, Christine (author)
- Johann Wolfgang Goethe Universität Frankfurt am Main,Goethe University Frankfurt,Chalmers tekniska högskola,Chalmers University of Technology
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- Pedersen, Anders, 1976 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg
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- Törnroth-Horsefield, Susanna, 1973 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg
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- Ökvist, Mats, 1970 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg
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- Karlsson, B Göran, 1962 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Rydström, Jan, 1943 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg
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- Krengel, Ute, 1964 (author)
- Chalmers tekniska högskola,Chalmers University of Technology,Universitetet i Oslo,University of Oslo
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(creator_code:org_t)
- Elsevier BV, 2005
- 2005
- English.
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In: Journal of molecular biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 352:2, s. 299-312
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Abstract
Subject headings
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- The dimeric integral membrane protein nicotinamide nucleotide transhydrogenase is required for cellular regeneration of NADPH in mitochondria and prokaryotes, for detoxification and biosynthesis purposes. Under physiological conditions, transhydrogenase couples the reversible reduction of NADP+ by NADH to an inward proton translocation across the membrane. Here, we present crystal structures of the NAD(H)-binding domain I of transhydrogenase from Escherichia coli, in the absence as well as in the presence of oxidized and reduced substrate. The structures were determined at 1.9-2.0 A resolution. Overall, the structures are highly similar to the crystal structure of a previously published NAD(H)-binding domain, from Rhodospirillum rubrum transhydrogenase. However, this particular domain is unique, since it is covalently connected to the integral-membrane part of transhydrogenase. Comparative studies between the structures of the two species reveal extensively differing surface properties and point to the possible importance of a rigid peptide (PAPP) in the connecting linker for conformational coupling. Further, the kinetic analysis of a deletion mutant, from which the protruding beta-hairpin was removed, indicates that this structural element is important for catalytic activity, but not for domain I:domain III interaction or dimer formation. Taken together, these results have important implications for the enzyme mechanism of the large group of transhydrogenases, including mammalian enzymes, which contain a connecting linker between domains I and II.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Binding Sites
- Computer Simulation
- Crystallography
- X-Ray
- Dimerization
- Escherichia coli
- chemistry
- Models
- Molecular
- NADP Transhydrogenase
- chemistry
- Protein Structure
- Tertiary
- Proton Pumps
- chemistry
- Protein Structure
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Johansson, Tomas
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Oswald, Christin ...
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Pedersen, Anders ...
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Törnroth-Horsefi ...
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Ökvist, Mats, 19 ...
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Karlsson, B Göra ...
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Rydström, Jan, 1 ...
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Krengel, Ute, 19 ...
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
- Articles in the publication
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Journal of molec ...
- By the university
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University of Gothenburg
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Chalmers University of Technology