2ivo
From Proteopedia
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| - | [[Image:2ivo. | + | [[Image:2ivo.jpg|left|200px]]<br /><applet load="2ivo" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ivo" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2ivo, resolution 2.90Å" /> | caption="2ivo, resolution 2.90Å" /> | ||
'''STRUCTURE OF UP1 PROTEIN'''<br /> | '''STRUCTURE OF UP1 PROTEIN'''<br /> | ||
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| + | ==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== | ==About this Structure== | ||
| - | 2IVO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with WO4 as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 2IVO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with WO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:Wo4 Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC3:Wo4 Binding Site For Chain B'>AC3</scene>, <scene name='pdbsite=AC4:Wo4 Binding Site For Chain C'>AC4</scene>, <scene name='pdbsite=AC6:Wo4 Binding Site For Chain D'>AC6</scene>, <scene name='pdbsite=AC8:Wo4 Binding Site For Chain A'>AC8</scene>, <scene name='pdbsite=AC9:Wo4 Binding Site For Chain C'>AC9</scene>, <scene name='pdbsite=BC1:Wo4 Binding Site For Chain A'>BC1</scene> and <scene name='pdbsite=BC2:Wo4 Binding Site For Chain B'>BC2</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IVO OCA]. |
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| + | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17766251 17766251] | ||
[[Category: Pyrococcus abyssi]] | [[Category: Pyrococcus abyssi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:36:41 2007'' |
Revision as of 17:26, 18 December 2007
|
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
2IVO is a Single protein structure of sequence from Pyrococcus abyssi with WO4 as ligand. 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 Tue Dec 18 19:36:41 2007
Categories: Pyrococcus abyssi | Single protein | Dorlet, P. | Forterre, P. | Graille, M. | Hecker, A. | Leulliot, N. | Quevillon-Cheruel, S. | Tilbeurgh, H.Van. | Ulryck, N. | WO4 | Fe/zn dependent nucleotide phosphatase | Hydrolase | Hypothetical protein | Metal-binding | Metalloprotease | Protease | Up1 keops complex | Zinc
