3ENC

Crystal structure of Pyrococcus furiosus PCC1 dimer

Summary for 3ENC

• Entry DOI: 10.2210/pdb3enc/pdb
• Related: 3EN9 3ENH 3ENO
• Descriptor: protein PCC1 (1 entity in total)
• Functional Keywords: dimerization domain, keops, telomere, unknown function
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 2
• Total formula weight: 20082.40

Authors

Neculai, D. (deposition date: 2008-09-25, release date: 2008-10-28, Last modification date: 2024-10-30)

Primary citation

Mao, D.Y.,Neculai, D.,Downey, M.,Orlicky, S.,Haffani, Y.Z.,Ceccarelli, D.F.,Ho, J.S.,Szilard, R.K.,Zhang, W.,Ho, C.S.,Wan, L.,Fares, C.,Rumpel, S.,Kurinov, I.,Arrowsmith, C.H.,Durocher, D.,Sicheri, F.
Atomic structure of the KEOPS complex: an ancient protein kinase-containing molecular machine.
Mol.Cell, 32:259-275, 2008

PubMed Abstract: Kae1 is a universally conserved ATPase and part of the essential gene set in bacteria. In archaea and eukaryotes, Kae1 is embedded within the protein kinase-containing KEOPS complex. Mutation of KEOPS subunits in yeast leads to striking telomere and transcription defects, but the exact biochemical function of KEOPS is not known. As a first step to elucidating its function, we solved the atomic structure of archaea-derived KEOPS complexes involving Kae1, Bud32, Pcc1, and Cgi121 subunits. Our studies suggest that Kae1 is regulated at two levels by the primordial protein kinase Bud32, which is itself regulated by Cgi121. Moreover, Pcc1 appears to function as a dimerization module, perhaps suggesting that KEOPS may be a processive molecular machine. Lastly, as Bud32 lacks the conventional substrate-recognition infrastructure of eukaryotic protein kinases including an activation segment, Bud32 may provide a glimpse of the evolutionary history of the protein kinase family.

PubMed: 18951093
DOI: 10.1016/j.molcel.2008.10.002

Experimental method

X-RAY DIFFRACTION (2.6304 Å)