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  Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold

Bauer, S., Kemter, K., Bacher, A., Huber, R., Fischer, M., & Steinbacher, S. (2003). Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold. Journal of Molecular Biology, 326(5), 1463-1473.

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Genre: Journal Article
Alternative Title : J. Mol. Biol.

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 Creators:
Bauer, S.1, Author              
Kemter, K., Author
Bacher, A., Author
Huber, R.1, Author              
Fischer, M., Author
Steinbacher, S.1, Author              
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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Free keywords: kinase; phosphoryl transferases; flavin cofactors; metal binding
 Abstract: The essential redox cofactors riboflavin monophosphate (FMN) and flavin adenine dinucleotide (FAD) are synthesised from their precursor, riboflavin, in sequential reactions by the metal-deppndent riboflavin kinase and FAD synthetase. Here, we describe the 1.6 Angstrom crystal structure of the Schizosaccharomyces pombe riboflavin kinase. The enzyme represents a novel family of phosphoryl transferring enzymes. It is a monomer comprising a central beta-barrel clasped on one side by two C-terminal helices that display an L-like shape. The opposite side of the beta-barrel serves as a platform for substrate binding as demonstrated by complexes with ADP and FMN. Formation of the ATP-binding site requires significant rearrangements in a short alpha-helix as compared to the substrate free form. The diphosphate moiety of ADP is covered by the glycine-rich flap I formed from parts of this a-helix. In contrast, no significant changes are observed upon binding of riboflavin. The ribityl side-chain might be covered by a rather flexible flap II. The unusual metal-binding site involves, in addition to the ADP phosphates, only the strictly conserved Thr45. This may explain the preference for zinc observed in vitro. (C) 2003 Elsevier Science Ltd. All rights reserved.

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Language(s): eng - English
 Dates: 2003-03-07
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41531
ISI: 000181698300014
 Degree: -

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Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 326 (5) Sequence Number: - Start / End Page: 1463 - 1473 Identifier: ISSN: 0022-2836