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The structure of the Escherichia coli nucleoside diphosphate kinase reveals a new quaternary architecture for this enzyme family
Author(s) -
Moynié Lucile,
Giraud MarieFrance,
Georgescauld Florian,
Lascu Ioan,
Dautant Alain
Publication year - 2007
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21316
Subject(s) - protein quaternary structure , tetramer , myxococcus xanthus , escherichia coli , nucleoside , chemistry , nucleoside diphosphate kinase , stereochemistry , protein subunit , transferase , biochemistry , crystallography , biology , kinase , enzyme , gene , mutant
Nucleoside diphosphate kinase (NDPK) catalyzes the transfer of γ‐phosphate from nucleoside triphosphates to nucleoside diphosphates. The subunit folding and the dimeric basic structural unit are remarkably the same for available structures but, depending on species, dimers self‐associate to form hexamers or tetramers. The crystal structure of the Escherichia coli NDPK reveals a new tetrameric quaternary structure for this protein family. The two tetramers differ by the relative orientation of interacting dimers, which face either the convex or the concave side of their central sheet as in either Myxococcus xanthus (type I) or E. coli (type II), respectively. In the type II tetramer, the subunits interact by a new interface harboring a zone called the Kpn loop as in hexamers, but by the opposite face of this loop. The evolutionary conservation of the interface residues indicates that this new quaternary structure seems to be the most frequent assembly mode in bacterial tetrameric NDP kinases. Proteins 2007. © 2007 Wiley‐Liss, Inc.