Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5C7P

Structure of Leishmania nucleoside diphostate kinase mutant P95S

Summary for 5C7P
Entry DOI10.2210/pdb5c7p/pdb
Related3NGS 5CAA 5CAB
DescriptorNucleoside diphosphate kinase (1 entity in total)
Functional Keywordsleishmania major, nucleoside diphosphate kinase, site-directed mutagenesis, quaternary structure, conformational stability, transferase
Biological sourceLeishmania major
Total number of polymer chains3
Total formula weight56466.85
Authors
Vieira, P.S.,de Giuseppe, P.O.,de Oliveira, A.H.C.,Murakami, M.T. (deposition date: 2015-06-24, release date: 2015-10-14, Last modification date: 2023-09-27)
Primary citationVieira, P.S.,de Giuseppe, P.O.,de Oliveira, A.H.,Murakami, M.T.
The role of the C-terminus and Kpn loop in the quaternary structure stability of nucleoside diphosphate kinase from Leishmania parasites.
J.Struct.Biol., 192:336-341, 2015
Cited by
PubMed Abstract: Nucleoside diphosphate kinase (NDK) is a housekeeping enzyme that plays key roles in nucleotide recycling and homeostasis in trypanosomatids. Moreover, it is secreted by the intracellular parasite Leishmania to modulate the host response. These functions make NDK an attractive target for drug design and for studies aiming at a better understanding of the mechanisms mediating host-pathogen interactions. Here, we report the crystal structures of three mutants of the NDK from Leishmania major (LmNDK) that affects the stability of the hexameric biological assembly including P95S, Δ5Ct (lacking the last five residues) and the double mutant P100S/Δ5Ct. Although P95S and Δ5Ct variants conserve the hexameric structure of the wild-type protein, the double mutant becomes a dimer as shown by in solution studies. Free energy calculation of dimer-dimer interfaces and enzymatic assays indicate that P95S, Δ5Ct and P100S/Δ5Ct mutations progressively decrease the hexamer stability and enzyme activity. These results demonstrate that the mutated regions play a role in protein function through stabilizing the quaternary arrangement.
PubMed: 26410384
DOI: 10.1016/j.jsb.2015.09.009
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.144 Å)
Structure validation

239803

数据于2025-08-06公开中

PDB statisticsPDBj update infoContact PDBjnumon