Structural highlights
Function[NDK_MYCTU] Major role in the synthesis of nucleoside triphosphates other than ATP.[HAMAP-Rule:MF_00451] Publication Abstract from PubMedThe crystal structure of the wild-type nucleoside diphosphate kinase from Mycobacterium tuberculosis at 2.6 A resolution revealed that the intersubunit salt bridge Arg80-Asp93 contributes to the thermal stability of the hexamer (Tm = 76 degrees C). On mutating Asp93 to Asn to break the salt bridge, the thermal stability dramatically decreased by 27.6 degrees C. Here, on mutating Arg80 to Asn, the thermal stability also significantly decreased by 8.0 degrees C. In the X-ray structure of the R80N mutant solved at 1.9 A 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. Structure of Mycobacterium tuberculosis nucleoside diphosphate kinase R80N mutant in complex with citrate.,Georgescauld F, Moynie L, Habersetzer J, Dautant A Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):40-3. doi:, 10.1107/S2053230X13034134. Epub 2013 Dec 24. PMID:24419614[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||||||
This page was last modified 08:43, 6 March 2019.