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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2003-2-21
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pubmed:databankReference |
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pubmed:abstractText |
The essential redox cofactors riboflavin monophosphate (FMN) and flavin adenine dinucleotide (FAD) are synthesised from their precursor, riboflavin, in sequential reactions by the metal-dependent riboflavin kinase and FAD synthetase. Here, we describe the 1.6A 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 alpha-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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
326
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1463-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12595258-Adenosine Diphosphate,
pubmed-meshheading:12595258-Adenosine Triphosphate,
pubmed-meshheading:12595258-Amino Acid Sequence,
pubmed-meshheading:12595258-Binding Sites,
pubmed-meshheading:12595258-Crystallization,
pubmed-meshheading:12595258-Crystallography, X-Ray,
pubmed-meshheading:12595258-Flavin Mononucleotide,
pubmed-meshheading:12595258-Models, Molecular,
pubmed-meshheading:12595258-Molecular Sequence Data,
pubmed-meshheading:12595258-Multienzyme Complexes,
pubmed-meshheading:12595258-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:12595258-Protein Binding,
pubmed-meshheading:12595258-Protein Conformation,
pubmed-meshheading:12595258-Protein Folding,
pubmed-meshheading:12595258-Riboflavin,
pubmed-meshheading:12595258-Schizosaccharomyces,
pubmed-meshheading:12595258-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:12595258-Sequence Homology, Amino Acid,
pubmed-meshheading:12595258-Substrate Specificity
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pubmed:year |
2003
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pubmed:articleTitle |
Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold.
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pubmed:affiliation |
Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152, Martinsried, Germany.
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pubmed:publicationType |
Journal Article,
In Vitro
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