1bhn
NUCLEOSIDE DIPHOSPHATE KINASE ISOFORM A FROM BOVINE RETINA
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OverviewOverview
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.
About this StructureAbout this Structure
1BHN is a Single protein structure of sequence from Bos taurus with 35G as ligand. Active as Nucleoside-diphosphate kinase, with EC number 2.7.4.6 Structure known Active Site: . Full crystallographic information is available from OCA.
ReferenceReference
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
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