X-RAY STRUCTURE OF NUCLEOSIDE DIPHOSPHATE KINASE

被引:185
作者
DUMAS, C
LASCU, I
MORERA, S
GLASER, P
FOURME, R
WALLET, V
LACOMBE, ML
VERON, M
JANIN, J
机构
[1] INST PASTEUR,UNITE REGULAT EXPRESS GENET,CNRS,URA 1129,F-75724 PARIS 15,FRANCE
[2] UNIV PARIS 11,CNRS,UTILISAT RAYONNEMENT ELECTROMAGNET LAB,F-91405 ORSAY,FRANCE
关键词
DICTYOSTELIUM-DISCOIDEUM; DROSOPHILA AWD; NM23; NUCLEOSIDE DIPHOSPHATE KINASE; X-RAY CRYSTALLOGRAPHY;
D O I
10.1002/j.1460-2075.1992.tb05397.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The X-ray structure of a point mutant of nucleoside diphosphate kinase (NDP kinase) from Dictyostelium discoideum has been determined to 2.2 angstrom resolution. The enzyme is a hexamer made of identical subunits with a novel mononucleotide binding fold. Each subunit contains an alpha/beta domain with a four stranded, antiparallel beta-sheet. The topology is different from adenylate kinase, but identical to the allosteric domain of Escherichia coli ATCase regulatory subunits, which bind mononucleotides at an equivalent position. Dimer contacts between NDP kinase subunits within the hexamer are similar to those in ATCase. Trimer contacts involve a large loop of polypeptide chain that bears the site of the Pro --> Ser substitution in Killer of prune (K-pn) mutants of the highly homologous Drosophila enzyme. Properties of Drosophila NDP kinase, the product of the awd developmental gene, and of the human enzyme, the product of the nm23 genes in tumorigenesis, are discussed in view of the three-dimensional structure and of possible interactions of NDP kinase with other nucleotide binding proteins.
引用
收藏
页码:3203 / 3208
页数:6
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