1zth

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[[Image:1zth.gif|left|200px]]<br /><applet load="1zth" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zth.gif|left|200px]]
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caption="1zth, resolution 1.89&Aring;" />
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'''Crystal Structure of A.fulgidus Rio1 serine protein kinase bound to ADP and Manganese ion'''<br />
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{{Structure
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|PDB= 1zth |SIZE=350|CAPTION= <scene name='initialview01'>1zth</scene>, resolution 1.89&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|ACTIVITY=
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|GENE= Rio1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])
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}}
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'''Crystal Structure of A.fulgidus Rio1 serine protein kinase bound to ADP and Manganese ion'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZTH OCA].
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1ZTH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZTH OCA].
==Reference==
==Reference==
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Structure and activity of the atypical serine kinase Rio1., Laronde-Leblanc N, Guszczynski T, Copeland T, Wlodawer A, FEBS J. 2005 Jul;272(14):3698-713. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16008568 16008568]
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Structure and activity of the atypical serine kinase Rio1., Laronde-Leblanc N, Guszczynski T, Copeland T, Wlodawer A, FEBS J. 2005 Jul;272(14):3698-713. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16008568 16008568]
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: rrna]]
[[Category: rrna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:18:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:39:39 2008''

Revision as of 13:39, 20 March 2008


PDB ID 1zth

Drag the structure with the mouse to rotate
, resolution 1.89Å
Ligands: and
Gene: Rio1 (Archaeoglobus fulgidus)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of A.fulgidus Rio1 serine protein kinase bound to ADP and Manganese ion


Overview

Rio1 is the founding member of the RIO family of atypical serine kinases that are universally present in all organisms from archaea to mammals. Activity of Rio1 was shown to be absolutely essential in Saccharomyces cerevisiae for the processing of 18S ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. We determined high-resolution crystal structures of Archaeoglobus fulgidus Rio1 in the presence and absence of bound nucleotides. Crystallization of Rio1 in the presence of ATP or ADP and manganese ions demonstrated major conformational changes in the active site, compared with the uncomplexed protein. Comparisons of the structure of Rio1 with the previously determined structure of the Rio2 kinase defined the minimal RIO domain and the distinct features of the RIO subfamilies. We report here that Ser108 represents the sole autophosphorylation site of A. fulgidus Rio1 and have therefore established its putative peptide substrate. In addition, we show that a mutant enzyme that cannot be autophosphorylated can still phosphorylate an inactive form of Rio1, as well as a number of typical kinase substrates.

About this Structure

1ZTH is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Structure and activity of the atypical serine kinase Rio1., Laronde-Leblanc N, Guszczynski T, Copeland T, Wlodawer A, FEBS J. 2005 Jul;272(14):3698-713. PMID:16008568

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