4XAH
X-ray crystal structure of S. cerevisiae Cgi121
Summary for 4XAH
| Entry DOI | 10.2210/pdb4xah/pdb |
| Descriptor | EKC/KEOPS complex subunit CGI121 (2 entities in total) |
| Functional Keywords | keops, cgi121, bud32-binding protein, protein binding |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Cellular location | Nucleus : Q03705 |
| Total number of polymer chains | 2 |
| Total formula weight | 43183.62 |
| Authors | Zhang, W.,Graille, M.,Collinet, B.,van Tilbeurgh, H. (deposition date: 2014-12-14, release date: 2015-03-18, Last modification date: 2024-11-13) |
| 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 Cited by 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: 25735745DOI: 10.1093/nar/gkv155 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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