4ANE

R80N MUTANT OF NUCLEOSIDE DIPHOSPHATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS

Summary for 4ANE

• Entry DOI: 10.2210/pdb4ane/pdb
• Related: 1K44 4ANC 4AND
• Descriptor: NUCLEOSIDE DIPHOSPHATE KINASE, CITRIC ACID (3 entities in total)
• Functional Keywords: transferase
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Cellular location: Cytoplasm (By similarity): P84284
• Total number of polymer chains: 6
• Total formula weight: 87452.64

Authors

Georgescauld, F.,Moynie, L.,Habersetzer, J.,Lascu, I.,Dautant, A. (deposition date: 2012-03-16, release date: 2013-03-13, Last modification date: 2023-12-20)

Primary citation

Georgescauld, F.,Moynie, L.,Habersetzer, J.,Dautant, A.
Structure of Mycobacterium Tuberculosis Nucleoside Diphosphate Kinase R80N Mutant in Complex with Citrate
Acta Crystallogr.,Sect.D, 70:40-, 2014

PubMed Abstract: The crystal structure of the wild-type nucleoside diphosphate kinase from Mycobacterium tuberculosis at 2.6 Å resolution revealed that the intersubunit salt bridge Arg80-Asp93 contributes to the thermal stability of the hexamer (Tm = 76°C). On mutating Asp93 to Asn to break the salt bridge, the thermal stability dramatically decreased by 27.6°C. Here, on mutating Arg80 to Asn, the thermal stability also significantly decreased by 8.0°C. In the X-ray structure of the R80N mutant solved at 1.9 Å resolution the salt bridge was replaced by intersubunit hydrogen bonds that contribute to the thermal stability of the hexamer. A citrate anion from the crystallization buffer was bound at the bottom of the nucleotide-binding site via electrostatic and hydrogen-bonding interactions with six conserved residues involved in nucleotide binding. Structural analysis shows that the citrate is present at the location of the nucleotide phosphate groups.

PubMed: 24419614
DOI: 10.1107/S2053230X13034134

Experimental method

X-RAY DIFFRACTION (1.9 Å)