2v9k
From Proteopedia
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==Overview== | ==Overview== | ||
- | Pseudouridine (Psi) synthases catalyze the formation of one or more | + | Pseudouridine (Psi) synthases catalyze the formation of one or more specific Psis in structured RNAs. Five families of Psi synthases have been characterized based on sequence homology. Pus10 has no significant sequence homology to these defined families and therefore represents a new family of Psi synthases. Initial characterization studies show that an archael Pus10 catalyzes the universally conserved Psi55 in tRNA. We present here the crystal structure of human Pus10 at 2.0 A resolution, which is the first structural description from this novel Psi synthase family. Pus10 is a crescent-shaped molecule with two domains, the universally conserved Psi synthase catalytic domain and a THUMP-containing domain, which is unique to the Pus10 family. Superposition of the catalytic domains of Pus10 and other Psi synthases identifies the full set of conserved Psi synthase active site residues indicating that Pus10 likely employs a similar catalytic mechanism to other Psi synthases. The Pus10 active site is located in a deep pocket of a basic cleft adjacent to flexible thumb and forefinger loops, which could provide further stabilization for binding the RNA substrate. Modeling studies demonstrate that the cleft between the catalytic and accessory domain is large enough and electrostatically compatible to accommodate an RNA stem and support the role of the N-terminal domain as an accessory RNA-binding domain. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | Crystal | + | Crystal structure of human Pus10, a novel pseudouridine synthase., McCleverty CJ, Hornsby M, Spraggon G, Kreusch A, J Mol Biol. 2007 Nov 9;373(5):1243-54. Epub 2007 Aug 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17900615 17900615] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hornsby, M.]] | [[Category: Hornsby, M.]] | ||
[[Category: Kreusch, A.]] | [[Category: Kreusch, A.]] | ||
- | [[Category: Mccleverty, C | + | [[Category: Mccleverty, C J.]] |
[[Category: Spraggon, G.]] | [[Category: Spraggon, G.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: thump domain]] | [[Category: thump domain]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:54:17 2008'' |
Revision as of 16:54, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN PUS10, A NOVEL PSEUDOURIDINE SYNTHASE.
Overview
Pseudouridine (Psi) synthases catalyze the formation of one or more specific Psis in structured RNAs. Five families of Psi synthases have been characterized based on sequence homology. Pus10 has no significant sequence homology to these defined families and therefore represents a new family of Psi synthases. Initial characterization studies show that an archael Pus10 catalyzes the universally conserved Psi55 in tRNA. We present here the crystal structure of human Pus10 at 2.0 A resolution, which is the first structural description from this novel Psi synthase family. Pus10 is a crescent-shaped molecule with two domains, the universally conserved Psi synthase catalytic domain and a THUMP-containing domain, which is unique to the Pus10 family. Superposition of the catalytic domains of Pus10 and other Psi synthases identifies the full set of conserved Psi synthase active site residues indicating that Pus10 likely employs a similar catalytic mechanism to other Psi synthases. The Pus10 active site is located in a deep pocket of a basic cleft adjacent to flexible thumb and forefinger loops, which could provide further stabilization for binding the RNA substrate. Modeling studies demonstrate that the cleft between the catalytic and accessory domain is large enough and electrostatically compatible to accommodate an RNA stem and support the role of the N-terminal domain as an accessory RNA-binding domain.
About this Structure
2V9K is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of human Pus10, a novel pseudouridine synthase., McCleverty CJ, Hornsby M, Spraggon G, Kreusch A, J Mol Biol. 2007 Nov 9;373(5):1243-54. Epub 2007 Aug 29. PMID:17900615
Page seeded by OCA on Thu Feb 21 18:54:17 2008
Categories: Homo sapiens | Single protein | Hornsby, M. | Kreusch, A. | Mccleverty, C J. | Spraggon, G. | CL | EPE | GOL | ZN | Lyase | Pseudouridine synthase | Pus10 | Rna modification | Thump domain