2ivn
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The Kae1 (Kinase-associated endopeptidase 1) protein is a member of the | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Leulliot, N.]] | [[Category: Leulliot, N.]] | ||
[[Category: Quevillon-Cheruel, S.]] | [[Category: Quevillon-Cheruel, S.]] | ||
| - | [[Category: Tilbeurgh, H | + | [[Category: Tilbeurgh, H Van.]] |
[[Category: Ulryck, N.]] | [[Category: Ulryck, N.]] | ||
[[Category: ANP]] | [[Category: ANP]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:27 2008'' |
Revision as of 15:56, 21 February 2008
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STRUCTURE OF UP1 PROTEIN
Overview
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.
About this Structure
2IVN is a Single protein structure of sequence from Pyrococcus abyssi with , and as ligands. Active as O-sialoglycoprotein endopeptidase, with EC number 3.4.24.57 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro., 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, Nucleic Acids Res. 2007;35(18):6042-51. Epub 2007 Aug 30. PMID:17766251
Page seeded by OCA on Thu Feb 21 17:56:27 2008
Categories: O-sialoglycoprotein endopeptidase | Pyrococcus abyssi | Single protein | Dorlet, P. | Forterre, P. | Graille, M. | Hecker, A. | Leulliot, N. | Quevillon-Cheruel, S. | Tilbeurgh, H Van. | Ulryck, N. | ANP | GOL | MG | Fe/zn dependent nucleotide phosphatase | Hydrolase | Hypothetical protein | Metal-binding | Metalloprotease | Protease | Up1 keops complex | Zinc
