2qgi
From Proteopedia
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The UDP complex structure of the sixth gene product of the F1-ATPase operon of Rhodobacter blasticus
Overview
The F(1)-ATP synthase atp operon in the proteobacterium Rhodobacter, blasticus contains six open reading frames, encoding six hypothetical, proteins. Five of these subunits, in the stoichiometry, (alphabeta)(3)gammadeltavarepsilon make up the catalytic F(1)-ATP synthase, complex similarly in bacteria, chloroplasts and mitochondria. The sixth, gene of the R. blasticus atp operon, urf6, shows very little sequence, homology to any protein of known structure or function. The gene has, previously been cloned, the product (called majastridin) has been, heterologously expressed in Escherichia coli, and purified to high, homogeneity [M. Brosche, I. Kalbina, M. Arnfelt, G. Benito, B.G. Karlsson, A. Strid, Occurrence, overexpression and partial purification of the, protein (majastridin) corresponding to the URF6 gene of the Rhodobacter, blasticus atp operon, Eur. J. Biochem. 255 (1998) 87-92]. We have solved, the X-ray crystal structure and refined a model of majastridin to atomic, resolution. Here we present the crystal structures of apo-majastridin and, the complex of majastridin with Mn(2+) and UDP and show that it has, extensive structural similarity to glycosyltransferases (EC 2.4). This is, the first structure determined from a new group of distantly related, bacterial proteins of at least six members. They share the identical amino, acids that bind Mn(2+) and a triplet of amino acids in the putative, sugar-binding site.
About this Structure
2QGI is a Single protein structure of sequence from Rhodobacter blasticus with and as ligands. Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
Crystal structure of a protein, structurally related to glycosyltransferases, encoded in the Rhodobacter blasticus atp operon., Enroth C, Strid A, Biochim Biophys Acta. 2007 Nov 19;. PMID:18067873
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