1BHN

NUCLEOSIDE DIPHOSPHATE KINASE ISOFORM A FROM BOVINE RETINA

Summary for 1BHN

• Entry DOI: 10.2210/pdb1bhn/pdb
• Descriptor: NUCLEOSIDE DIPHOSPHATE TRANSFERASE, GUANOSINE-3',5'-MONOPHOSPHATE, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: phosphotransferase
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm : P52174
• Total number of polymer chains: 6
• Total formula weight: 108440.17

Authors

Ladner, J.E.,Abdulaev, N.G.,Kakuev, D.L.,Karaschuk, G.N.,Tordova, M.,Eisenstein, E.,Fujiwara, J.H.,Ridge, K.D.,Gilliland, G.L. (deposition date: 1998-06-10, release date: 1999-02-16, Last modification date: 2024-04-03)

Primary citation

Ladner, J.E.,Abdulaev, N.G.,Kakuev, D.L.,Tordova, M.,Ridge, K.D.,Gilliland, G.L.
The three-dimensional structures of two isoforms of nucleoside diphosphate kinase from bovine retina.
Acta Crystallogr.,Sect.D, 55:1127-1135, 1999

PubMed Abstract: 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.

PubMed: 10329774
DOI: 10.1107/S0907444999002528

Experimental method

X-RAY DIFFRACTION (2.4 Å)