1p9q

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(New page: 200px<br /><applet load="1p9q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9q, resolution 2.00&Aring;" /> '''Structure of a hypot...)
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'''Structure of a hypothetical protein AF0491 from Archaeoglobus fulgidus'''<br />
'''Structure of a hypothetical protein AF0491 from Archaeoglobus fulgidus'''<br />
==Overview==
==Overview==
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A combination of structural, biochemical, and genetic studies in model, organisms was used to infer a cellular role for the human protein (SBDS), responsible for Shwachman-Bodian-Diamond syndrome. The crystal structure, of the SBDS homologue in Archaeoglobus fulgidus, AF0491, revealed a three, domain protein. The N-terminal domain, which harbors the majority of, disease-linked mutations, has a novel three-dimensional fold. The central, domain has the common winged helix-turn-helix motif, and the C-terminal, domain shares structural homology with known RNA-binding domains., Proteomic analysis of the SBDS sequence homologue in Saccharomyces, cerevisiae, YLR022C, revealed an association with over 20 proteins, involved in ribosome biosynthesis. NMR structural genomics revealed, another yeast protein, YHR087W, to be a structural homologue of the AF0491, N-terminal domain. Sequence analysis confirmed them as distant sequence, homologues, therefore related by divergent evolution. Synthetic genetic, array analysis of YHR087W revealed genetic interactions with proteins, involved in RNA and rRNA processing including Mdm20/Nat3, Nsr1, and Npl3., Our observations, taken together with previous reports, support the, conclusion that SBDS and its homologues play a role in RNA metabolism.
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A combination of structural, biochemical, and genetic studies in model organisms was used to infer a cellular role for the human protein (SBDS) responsible for Shwachman-Bodian-Diamond syndrome. The crystal structure of the SBDS homologue in Archaeoglobus fulgidus, AF0491, revealed a three domain protein. The N-terminal domain, which harbors the majority of disease-linked mutations, has a novel three-dimensional fold. The central domain has the common winged helix-turn-helix motif, and the C-terminal domain shares structural homology with known RNA-binding domains. Proteomic analysis of the SBDS sequence homologue in Saccharomyces cerevisiae, YLR022C, revealed an association with over 20 proteins involved in ribosome biosynthesis. NMR structural genomics revealed another yeast protein, YHR087W, to be a structural homologue of the AF0491 N-terminal domain. Sequence analysis confirmed them as distant sequence homologues, therefore related by divergent evolution. Synthetic genetic array analysis of YHR087W revealed genetic interactions with proteins involved in RNA and rRNA processing including Mdm20/Nat3, Nsr1, and Npl3. Our observations, taken together with previous reports, support the conclusion that SBDS and its homologues play a role in RNA metabolism.
==About this Structure==
==About this Structure==
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1P9Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P9Q OCA].
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1P9Q is a [http://en.wikipedia.org/wiki/Single_protein 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=1P9Q OCA].
==Reference==
==Reference==
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[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arrowsmith, C.H.]]
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[[Category: Arrowsmith, C H.]]
[[Category: Bochkarev, A.]]
[[Category: Bochkarev, A.]]
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[[Category: Edwards, A.M.]]
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[[Category: Edwards, A M.]]
[[Category: Evdokimova, E.]]
[[Category: Evdokimova, E.]]
[[Category: Savchenko, A.]]
[[Category: Savchenko, A.]]
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[[Category: unknown function]]
[[Category: unknown function]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:37:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:38 2008''

Revision as of 12:26, 21 February 2008


1p9q, resolution 2.00Å

Drag the structure with the mouse to rotate

Structure of a hypothetical protein AF0491 from Archaeoglobus fulgidus

Overview

A combination of structural, biochemical, and genetic studies in model organisms was used to infer a cellular role for the human protein (SBDS) responsible for Shwachman-Bodian-Diamond syndrome. The crystal structure of the SBDS homologue in Archaeoglobus fulgidus, AF0491, revealed a three domain protein. The N-terminal domain, which harbors the majority of disease-linked mutations, has a novel three-dimensional fold. The central domain has the common winged helix-turn-helix motif, and the C-terminal domain shares structural homology with known RNA-binding domains. Proteomic analysis of the SBDS sequence homologue in Saccharomyces cerevisiae, YLR022C, revealed an association with over 20 proteins involved in ribosome biosynthesis. NMR structural genomics revealed another yeast protein, YHR087W, to be a structural homologue of the AF0491 N-terminal domain. Sequence analysis confirmed them as distant sequence homologues, therefore related by divergent evolution. Synthetic genetic array analysis of YHR087W revealed genetic interactions with proteins involved in RNA and rRNA processing including Mdm20/Nat3, Nsr1, and Npl3. Our observations, taken together with previous reports, support the conclusion that SBDS and its homologues play a role in RNA metabolism.

About this Structure

1P9Q is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism., Savchenko A, Krogan N, Cort JR, Evdokimova E, Lew JM, Yee AA, Sanchez-Pulido L, Andrade MA, Bochkarev A, Watson JD, Kennedy MA, Greenblatt J, Hughes T, Arrowsmith CH, Rommens JM, Edwards AM, J Biol Chem. 2005 May 13;280(19):19213-20. Epub 2005 Feb 8. PMID:15701634

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