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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):425-9. doi: 10.1107/S1744309113005356. Epub 2013 Mar 28.

Crystallization and preliminary X-ray diffraction analysis of a DING protein from Pseudomonas aeruginosa PA14.

Author information

1
Aix-Marseille Université, URMITE, UM63, CNRS 7278, IRD 198, Inserm 1095, 27 Boulevard Jean Moulin, 13385 Marseille CEDEX 5, France.

Abstract

DING proteins form an emergent family of proteins consisting of an increasing number of homologues that have been identified in all kingdoms of life. They belong to the superfamily of phosphate-binding proteins and exhibit a high affinity for phosphate. In eukaryotes, DING proteins have been isolated by virtue of their implication in several diseases and biological processes. Some of them are potent inhibitors of HIV-1 replication/transcription, raising the question of their potential involvement in the human defence system. Recently, a protein from Pseudomonas aeruginosa strain PA14, named PA14DING or LapC, belonging to the DING family has been identified. The structure of PA14DING, combined with detailed biochemical characterization and comparative analysis with available DING protein structures, will be helpful in understanding the structural determinants implicated in the inhibition of HIV-1 by DING proteins. Here, the expression, purification and crystallization of PA14DING and the collection of X-ray data to 1.9 Å resolution are reported.

KEYWORDS:

DING proteins; HIV; antivirals; phosphate-binding proteins; virulence factors

PMID:
23545651
PMCID:
PMC3614170
DOI:
10.1107/S1744309113005356
[Indexed for MEDLINE]
Free PMC Article

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