1tqp
From Proteopedia
(New page: 200px<br /><applet load="1tqp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tqp, resolution 2.10Å" /> '''Crystal Structure of...) |
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| - | [[Image:1tqp.gif|left|200px]]<br /><applet load="1tqp" size=" | + | [[Image:1tqp.gif|left|200px]]<br /><applet load="1tqp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tqp, resolution 2.10Å" /> | caption="1tqp, resolution 2.10Å" /> | ||
'''Crystal Structure of A. fulgidus Rio2 Serine Protein Kinase Bound to ATP'''<br /> | '''Crystal Structure of A. fulgidus Rio2 Serine Protein Kinase Bound to ATP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The RIO family of atypical serine/threonine kinases contains two | + | The RIO family of atypical serine/threonine kinases contains two subfamilies, Rio1 and Rio2, highly conserved from archaea to man. Both RIO proteins from Saccharomyces cerevisiae catalyze serine phosphorylation in vitro, and the presence of conserved catalytic residues is required for cell viability. The activity of Rio2 is necessary for rRNA cleavage in 40S ribosomal subunit maturation. We solved the X-ray crystal structure of Archaeoglobus fulgidus Rio2, with and without bound nucleotides, at 2.0 A resolution. The C-terminal RIO domain is indeed structurally homologous to protein kinases, although it differs from known serine kinases in ATP binding and lacks the regions important for substrate binding. Unexpectedly, the N-terminal Rio2-specific domain contains a winged helix fold, seen primarily in DNA-binding proteins. These discoveries have implications in determining the target and function of RIO proteins and define a distinct new family of protein kinases. |
==About this Structure== | ==About this Structure== | ||
| - | 1TQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_dsm_4304 Archaeoglobus fulgidus dsm 4304] with ATP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_dsm_4304 Archaeoglobus fulgidus dsm 4304] with <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: serine kinase]] | [[Category: serine kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:25 2008'' |
Revision as of 13:16, 21 February 2008
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Crystal Structure of A. fulgidus Rio2 Serine Protein Kinase Bound to ATP
Overview
The RIO family of atypical serine/threonine kinases contains two subfamilies, Rio1 and Rio2, highly conserved from archaea to man. Both RIO proteins from Saccharomyces cerevisiae catalyze serine phosphorylation in vitro, and the presence of conserved catalytic residues is required for cell viability. The activity of Rio2 is necessary for rRNA cleavage in 40S ribosomal subunit maturation. We solved the X-ray crystal structure of Archaeoglobus fulgidus Rio2, with and without bound nucleotides, at 2.0 A resolution. The C-terminal RIO domain is indeed structurally homologous to protein kinases, although it differs from known serine kinases in ATP binding and lacks the regions important for substrate binding. Unexpectedly, the N-terminal Rio2-specific domain contains a winged helix fold, seen primarily in DNA-binding proteins. These discoveries have implications in determining the target and function of RIO proteins and define a distinct new family of protein kinases.
About this Structure
1TQP is a Single protein structure of sequence from Archaeoglobus fulgidus dsm 4304 with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases., LaRonde-LeBlanc N, Wlodawer A, Structure. 2004 Sep;12(9):1585-94. PMID:15341724
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