2aus
From Proteopedia
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| - | [[Image:2aus.gif|left|200px]] | + | [[Image:2aus.gif|left|200px]] |
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| - | '''Crystal structure of the archaeal box H/ACA sRNP Nop10-Cbf5 complex''' | + | {{Structure |
| + | |PDB= 2aus |SIZE=350|CAPTION= <scene name='initialview01'>2aus</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the archaeal box H/ACA sRNP Nop10-Cbf5 complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AUS is a [ | + | 2AUS is a [[Protein complex]] structure of sequences 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=2AUS OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5-aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity., Manival X, Charron C, Fourmann JB, Godard F, Charpentier B, Branlant C, Nucleic Acids Res. 2006 Feb 2;34(3):826-39. Print 2006. PMID:[http:// | + | Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5-aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity., Manival X, Charron C, Fourmann JB, Godard F, Charpentier B, Branlant C, Nucleic Acids Res. 2006 Feb 2;34(3):826-39. Print 2006. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16456033 16456033] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pyrococcus abyssi]] | [[Category: Pyrococcus abyssi]] | ||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:54:03 2008'' |
Revision as of 13:54, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the archaeal box H/ACA sRNP Nop10-Cbf5 complex
Overview
In archaeal rRNAs, the isomerization of uridine into pseudouridine (Psi) is achieved by the H/ACA sRNPs and the minimal set of proteins required for RNA:Psi-synthase activity is the aCBF5-aNOP10 protein pair. The crystal structure of the aCBF5-aNOP10 heterodimer from Pyrococcus abyssi was solved at 2.1 A resolution. In this structure, protein aNOP10 has an extended shape, with a zinc-binding motif at the N-terminus and an alpha-helix at the C-terminus. Both motifs contact the aCBF5 catalytic domain. Although less efficiently as does the full-length aNOP10, the aNOP10 C-terminal domain binds aCBF5 and stimulates the RNA-guided activity. We show that the C-terminal domain of aCBF5 (the PUA domain), which is wrapped by an N-terminal extension of aCBF5, plays a crucial role for aCBF5 binding to the guide sRNA. Addition of this domain in trans partially complement particles assembled with an aCBF5DeltaPUA truncated protein. In the crystal structure, the aCBF5-aNOP10 complex forms two kinds of heterotetramers with parallel and perpendicular orientations of the aNOP10 terminal alpha-helices, respectively. By gel filtration assay, we showed that aNOP10 can dimerize in solution. As both residues Y41 and L48 were needed for dimerization, the dimerization likely takes place by interaction of parallel alpha-helices.
About this Structure
2AUS is a Protein complex structure of sequences from Pyrococcus abyssi. Full crystallographic information is available from OCA.
Reference
Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5-aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity., Manival X, Charron C, Fourmann JB, Godard F, Charpentier B, Branlant C, Nucleic Acids Res. 2006 Feb 2;34(3):826-39. Print 2006. PMID:16456033
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