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Publication Abstract from PubMed

The crystal structures of two isoforms of nucleoside diphosphate kinase from bovine retina overexpressed in Escherischia coli have been determined to 2.4 A resolution. Both the isoforms, NBR-A and NBR-B, are hexameric and the fold of the monomer is in agreement with NDP-kinase structures from other biological sources. Although the polypeptide chains of the two isoforms differ by only two residues, they crystallize in different space groups. NBR-A crystallizes in space group P212121 with an entire hexamer in the asymmetric unit, while NBR-B crystallizes in space group P43212 with a trimer in the asymmetric unit. The highly conserved nucleotide-binding site observed in other nucleoside diphosphate kinase structures is also observed here. Both NBR-A and NBR-B were crystallized in the presence of cGMP. The nucleotide is bound with the base in the anti conformation. The NBR-A active site contained both cGMP and GDP each bound at half occupancy. Presumably, NBR-A had retained GDP (or GTP) from the purification process. The NBR-B active site contained only cGMP.

The three-dimensional structures of two isoforms of nucleoside diphosphate kinase from bovine retina.,Ladner JE, Abdulaev NG, Kakuev DL, Tordova M, Ridge KD, Gilliland GL Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1127-35. PMID:10329774^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.