3RK0

X-ray crystal Structure of the putative N-type ATP pyrophosphatase (PF0828) in complex with AMP from Pyrococcus furiosus, Northeast Structural Genomics Consortium Target PfR23

Replaces:  3H7E

Summary for 3RK0

• Entry DOI: 10.2210/pdb3rk0/pdb
• Related: 3RJZ 3RK1
• Descriptor: N-type ATP pyrophosphatase superfamily, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: structural genomics, psi-biology, northeast structural genomics consortium, nesg, alpha-beta protein that binds atp, possibly n-type atp pyrophosphatase, amp and atp binding, hydrolase
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 1
• Total formula weight: 27454.55

Authors

Forouhar, F.,Saadat, N.,Hussain, M.,Seetharaman, J.,Janjua, J.,Xiao, R.,Cunningham, K.,Ma, L.,Shastry, R.,Everett, J.K.,Nair, R.,Acton, T.B.,Rost, B.,Montelione, G.T.,Hunt, J.F.,Tong, L.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2011-04-16, release date: 2011-05-11, Last modification date: 2024-10-30)

Primary citation

Forouhar, F.,Saadat, N.,Hussain, M.,Seetharaman, J.,Lee, I.,Janjua, H.,Xiao, R.,Shastry, R.,Acton, T.B.,Montelione, G.T.,Tong, L.
A large conformational change in the putative ATP pyrophosphatase PF0828 induced by ATP binding.
Acta Crystallogr.,Sect.F, 67:1323-1327, 2011

PubMed Abstract: ATP pyrophosphatases (ATP PPases) are widely distributed in archaea and eukaryotes. They share an HUP domain at the N-terminus with a conserved PP-motif that interacts with the phosphates of ATP. The PF0828 protein from Pyrococcus furiosus is a member of the ATP PPase superfamily and it also has a 100-residue C-terminal extension that contains a strictly conserved EGG(E/D)xE(T/S) motif, which has been named the EGT-motif. Here, crystal structures of PF0828 alone and in complex with ATP or AMP are reported. The HUP domain contains a central five-stranded β-sheet that is surrounded by four helices, as in other related structures. The C-terminal extension forms a separate domain, named the EGT domain, which makes tight interactions with the HUP domain, bringing the EGT-motif near to the PP-motif and defining the putative active site of PF0828. Both motifs interact with the phosphate groups of ATP. A loop in the HUP domain undergoes a large conformational change to recognize the adenine base of ATP. In solution and in the crystal PF0828 is a dimer formed by the side-by-side arrangement of the HUP domains of the two monomers. The putative active site is located far from the dimer interface.

PubMed: 22102225
DOI: 10.1107/S1744309111031447

Experimental method

X-RAY DIFFRACTION (2.4 Å)