4WW7

Crystal structure of binary complex Bud32-Cgi121 in complex with AMP

Summary for 4WW7

• Entry DOI: 10.2210/pdb4ww7/pdb
• Descriptor: EKC/KEOPS complex subunit BUD32, EKC/KEOPS complex subunit CGI121, ADENOSINE MONOPHOSPHATE, ... (6 entities in total)
• Functional Keywords: keops, binary complex, bud32-cgi121, trna t6a, transferase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasm : P53323; Nucleus : Q03705
• Total number of polymer chains: 2
• Total formula weight: 52369.66

Authors

Zhang, W.,van Tilbeurgh, H. (deposition date: 2014-11-10, release date: 2015-03-18, Last modification date: 2024-05-01)

Primary citation

Zhang, W.,Collinet, B.,Graille, M.,Daugeron, M.C.,Lazar, N.,Libri, D.,Durand, D.,van Tilbeurgh, H.
Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex.
Nucleic Acids Res., 43:3358-3372, 2015

PubMed Abstract: The yeast KEOPS protein complex comprising Kae1, Bud32, Cgi121, Pcc1 and Gon7 is responsible for the essential tRNA threonylcarbamoyladenosine (t(6)A) modification. Deletion of genes coding for the KEOPS subunits also affects telomere elongation and transcriptional regulation. In the present work, the crystal structure of Bud32/Cgi121 in complex with ADP revealed that ADP is bound in the catalytic site of Bud32 in a canonical manner characteristic of Protein Kinase A (PKA) family proteins. We found that Gon7 forms a stable heterodimer with Pcc1 and report the crystal structure of the Pcc1-Gon7 heterodimer. Gon7 interacts with the same Pcc1 region engaged in the archaeal Pcc1 homodimer. We further show that yeast KEOPS, unlike its archaeal counterpart, exists as a heteropentamer in which Gon7, Pcc1, Kae1, Bud32 and Cgi121 also adopt a linear arrangement. We constructed a model of yeast KEOPS that provides structural insight into the role of Gon7. The model also revealed the presence of a highly positively charged crater surrounding the entrance of Kae1 that likely binds tRNA.

PubMed: 25735745
DOI: 10.1093/nar/gkv155

Experimental method

X-RAY DIFFRACTION (1.669 Å)