2ivn

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[[Image:2ivn.jpg|left|200px]]<br /><applet load="2ivn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ivn.jpg|left|200px]]
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caption="2ivn, resolution 1.65&Aring;" />
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'''STRUCTURE OF UP1 PROTEIN'''<br />
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{{Structure
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|PDB= 2ivn |SIZE=350|CAPTION= <scene name='initialview01'>2ivn</scene>, resolution 1.65&Aring;
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Anp+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Mg+Binding+Site+For+Chain+A'>AC3</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/O-sialoglycoprotein_endopeptidase O-sialoglycoprotein endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.57 3.4.24.57]
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|GENE=
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}}
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'''STRUCTURE OF UP1 PROTEIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2IVN 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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ANP:'>ANP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/O-sialoglycoprotein_endopeptidase O-sialoglycoprotein endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.57 3.4.24.57] Known structural/functional Sites: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Anp+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Mg+Binding+Site+For+Chain+A'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IVN OCA].
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2IVN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IVN OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/17766251 17766251]
[[Category: O-sialoglycoprotein endopeptidase]]
[[Category: O-sialoglycoprotein endopeptidase]]
[[Category: Pyrococcus abyssi]]
[[Category: Pyrococcus abyssi]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:33:54 2008''

Revision as of 15:33, 20 March 2008

Image:2ivn.jpg


PDB ID 2ivn

Drag the structure with the mouse to rotate
, resolution 1.65Å
Sites: , and
Ligands: , and
Activity: O-sialoglycoprotein endopeptidase, with EC number 3.4.24.57
Coordinates: save as pdb, mmCIF, xml



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. 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

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