2ohf
From Proteopedia
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Crystal structure of human OLA1 in complex with AMPPCP
Overview
Purine nucleotide binding proteins build the large family of P-loop, GTPases and related ATPases, which perform essential functions in all, kingdoms of life. The Obg family comprises a group of ancient GTPases, belonging to the TRAFAC (for translation factors) class and can be, subdivided into several distinct protein subfamilies. The founding member, of one of these subfamilies is the bacterial P-loop NTPase YchF, which had, so far been assumed to act as GTPase. We have biochemically characterized, the human homologue of YchF and found that it binds and hydrolyzes ATP, more efficiently than GTP. For this reason, we have termed the protein, hOLA1, for human Obg-like ATPase 1. Further biochemical characterization, of YchF proteins from different species revealed that ATPase activity is a, general but previously missed feature of the YchF subfamily of Obg-like, GTPases. To explain ATP specificity of hOLA1, we have solved the X-ray, structure of hOLA1 bound to the non-hydrolysable ATP analogue AMPPCP. Our, structural data help to explain the altered nucleotide specificity of YchF, homologues and identify the Ola/YchF subfamily of the Obg-related NTPases, as an exceptional example of a single protein subfamily, which has evolved, altered nucleotide specificity within a distinct protein family of, GTPases.
About this Structure
2OHF is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Human OLA1 defines an ATPase subfamily in the OBG family of GTP-binding proteins., Koller-Eichhorn R, Marquardt T, Gail R, Wittinghofer A, Kostrewa D, Kutay U, Kambach C, J Biol Chem. 2007 Apr 12;. PMID:17430889
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