1BHN

NUCLEOSIDE DIPHOSPHATE KINASE ISOFORM A FROM BOVINE RETINA

1BHN の概要

• エントリーDOI: 10.2210/pdb1bhn/pdb
• 分子名称: NUCLEOSIDE DIPHOSPHATE TRANSFERASE, GUANOSINE-3',5'-MONOPHOSPHATE, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: phosphotransferase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cytoplasm : P52174
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 108440.17

構造登録者

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. (登録日: 1998-06-10, 公開日: 1999-02-16, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)