Change search
ReferencesLink to record
Permanent link

Direct link
The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6 A resolution
Södertörn University, Avdelning Naturvetenskap.
2003 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 331, no 5, 1053-1063 p.Article in journal (Refereed) Published
Abstract [en]

Riboflavin synthase of Escherichia coli is a homotrimer with a molecular mass of 70 kDa. The enzyme catalyzes the dismutation of 6,7-dimethyl-8(1'-D-ribityl)-lumazine, affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. The N-terminal segment (residues 1-87) and the C-terminal segment (residues 98-187) form beta-barrels with similar fold and a high degree of sequence similarity. A recombinant peptide comprising amino acid residues 1-97 forms a dimer, which binds riboflavin with high affinity. Here,we report the structure of this construct in complex with riboflavin at 2.6 Angstrom resolution. It is demonstrated that the complex can serve as a model for ligand-binding in the native enzyme. The structure and riboflavin-binding mode is in excellent agreement with structural information obtained from the native enzyme from Escherichia coli and riboflavin synthase from Schizosaccharomyces pombe. The implications for the binding specificity and the regiospecificity of the catalyzed reaction are discussed.

Place, publisher, year, edition, pages
2003. Vol. 331, no 5, 1053-1063 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:sh:diva-15536DOI: 10.1016/S0022-2836(03)00844-1ISI: 000185036400009PubMedID: 12927541ScopusID: 2-s2.0-0042567586OAI: diva2:504740
Available from: 2012-02-21 Created: 2012-02-21 Last updated: 2014-04-16Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedScopus

Search in DiVA

By author/editor
Meining, Winfried
By organisation
Avdelning Naturvetenskap
In the same journal
Journal of Molecular Biology
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 33 hits
ReferencesLink to record
Permanent link

Direct link