2HUR

Escherichia coli nucleoside diphosphate kinase

Summary for 2HUR

• Entry DOI: 10.2210/pdb2hur/pdb
• Related: 1NPK 2NCK
• Descriptor: NUCLEOSIDE DIPHOSPHATE KINASE, SULFATE ION (3 entities in total)
• Functional Keywords: type ii tetramer, signaling protein, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A763
• Total number of polymer chains: 6
• Total formula weight: 92677.63

Authors

Moynie, L.,Giraud, M.-F.,Georgescauld, F.,Lascu, I.,Dautant, A. (deposition date: 2006-07-27, release date: 2007-04-10, Last modification date: 2023-08-30)

Primary citation

Moynie, L.,Giraud, M.-F.,Georgescauld, F.,Lascu, I.,Dautant, A.
The structure of the Escherichia coli nucleoside diphosphate kinase reveals a new quaternary architecture for this enzyme family
Proteins, 67:755-765, 2007

PubMed Abstract: Nucleoside diphosphate kinase (NDPK) catalyzes the transfer of gamma-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.

PubMed: 17330300
DOI: 10.1002/prot.21316

Experimental method

X-RAY DIFFRACTION (1.62 Å)