2IVP
Structure of UP1 protein
Summary for 2IVP
| Entry DOI | 10.2210/pdb2ivp/pdb |
| Related | 2IVN 2IVO |
| Descriptor | O-SIALOGLYCOPROTEIN ENDOPEPTIDASE, FE (II) ION, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | up1 keops complex, fe/zn dependent nucleotide phosphatase, metalloprotease, hypothetical protein, zinc, protease, hydrolase, metal-binding |
| Biological source | PYROCOCCUS ABYSSI |
| Total number of polymer chains | 1 |
| Total formula weight | 36807.85 |
| Authors | Hecker, A.,Leulliot, N.,Graille, M.,Dorlet, P.,Quevillon-Cheruel, S.,Ulryck, N.,Van Tilbeurgh, H.,Forterre, P. (deposition date: 2006-06-14, release date: 2007-07-31, Last modification date: 2024-05-08) |
| Primary citation | Hecker, A.,Leulliot, N.,Gadelle, D.,Graille, M.,Justome, A.,Dorlet, P.,Brochier, C.,Quevillon-Cheruel, S.,Le Cam, E.,Van Tilbeurgh, H.,Forterre, P. An Archaeal Orthologue of the Universal Protein Kae1 is an Iron Metalloprotein which Exhibits Atypical DNA-Binding Properties and Apurinic-Endonuclease Activity in Vitro. Nucleic Acids Res., 35:6042-, 2007 Cited by PubMed Abstract: The Kae1 (Kinase-associated endopeptidase 1) protein is a member of the recently identified transcription complex EKC and telomeres maintenance complex KEOPS in yeast. Kae1 homologues are encoded by all sequenced genomes in the three domains of life. Although annotated as putative endopeptidases, the actual functions of these universal proteins are unknown. Here we show that the purified Kae1 protein (Pa-Kae1) from Pyrococcus abyssi is an iron-protein with a novel type of ATP-binding site. Surprisingly, this protein did not exhibit endopeptidase activity in vitro but binds cooperatively to single and double-stranded DNA and induces unusual DNA conformational change. Furthermore, Pa-Kae1 exhibits a class I apurinic (AP)-endonuclease activity (AP-lyase). Both DNA binding and AP-endonuclease activity are inhibited by ATP. Kae1 is thus a novel and atypical universal DNA interacting protein whose importance could rival those of RecA (RadA/Rad51) in the maintenance of genome integrity in all living cells. PubMed: 17766251DOI: 10.1093/NAR/GKM554 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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