1i8f

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(New page: 200px<br /><applet load="1i8f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i8f, resolution 1.75&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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[[Image:1i8f.jpg|left|200px]]<br /><applet load="1i8f" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1i8f, resolution 1.75&Aring;" />
caption="1i8f, resolution 1.75&Aring;" />
'''THE CRYSTAL STRUCTURE OF A HEPTAMERIC ARCHAEAL SM PROTEIN: IMPLICATIONS FOR THE EUKARYOTIC SNRNP CORE'''<br />
'''THE CRYSTAL STRUCTURE OF A HEPTAMERIC ARCHAEAL SM PROTEIN: IMPLICATIONS FOR THE EUKARYOTIC SNRNP CORE'''<br />
==Overview==
==Overview==
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Sm proteins form the core of small nuclear ribonucleoprotein particles, (snRNPs), making them key components of several mRNA-processing, assemblies, including the spliceosome. We report the 1.75-A crystal, structure of SmAP, an Sm-like archaeal protein that forms a heptameric, ring perforated by a cationic pore. In addition to providing direct, evidence for such an assembly in eukaryotic snRNPs, this structure (i), shows that SmAP homodimers are structurally similar to human Sm, heterodimers, (ii) supports a gene duplication model of Sm protein, evolution, and (iii) offers a model of SmAP bound to single-stranded RNA, (ssRNA) that explains Sm binding-site specificity. The pronounced, electrostatic asymmetry of the SmAP surface imparts directionality to, putative SmAP-RNA interactions.
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Sm proteins form the core of small nuclear ribonucleoprotein particles (snRNPs), making them key components of several mRNA-processing assemblies, including the spliceosome. We report the 1.75-A crystal structure of SmAP, an Sm-like archaeal protein that forms a heptameric ring perforated by a cationic pore. In addition to providing direct evidence for such an assembly in eukaryotic snRNPs, this structure (i) shows that SmAP homodimers are structurally similar to human Sm heterodimers, (ii) supports a gene duplication model of Sm protein evolution, and (iii) offers a model of SmAP bound to single-stranded RNA (ssRNA) that explains Sm binding-site specificity. The pronounced electrostatic asymmetry of the SmAP surface imparts directionality to putative SmAP-RNA interactions.
==About this Structure==
==About this Structure==
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1I8F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I8F OCA].
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1I8F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I8F OCA].
==Reference==
==Reference==
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[[Category: Eisenberg, D.]]
[[Category: Eisenberg, D.]]
[[Category: Mura, C.]]
[[Category: Mura, C.]]
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[[Category: Sawaya, M.R.]]
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[[Category: Sawaya, M R.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: beta barrel-like smap monomers form 35-stranded beta-sheet in the heptamer]]
[[Category: beta barrel-like smap monomers form 35-stranded beta-sheet in the heptamer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:45:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:09 2008''

Revision as of 11:09, 21 February 2008


1i8f, resolution 1.75Å

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THE CRYSTAL STRUCTURE OF A HEPTAMERIC ARCHAEAL SM PROTEIN: IMPLICATIONS FOR THE EUKARYOTIC SNRNP CORE

Overview

Sm proteins form the core of small nuclear ribonucleoprotein particles (snRNPs), making them key components of several mRNA-processing assemblies, including the spliceosome. We report the 1.75-A crystal structure of SmAP, an Sm-like archaeal protein that forms a heptameric ring perforated by a cationic pore. In addition to providing direct evidence for such an assembly in eukaryotic snRNPs, this structure (i) shows that SmAP homodimers are structurally similar to human Sm heterodimers, (ii) supports a gene duplication model of Sm protein evolution, and (iii) offers a model of SmAP bound to single-stranded RNA (ssRNA) that explains Sm binding-site specificity. The pronounced electrostatic asymmetry of the SmAP surface imparts directionality to putative SmAP-RNA interactions.

About this Structure

1I8F is a Single protein structure of sequence from Pyrobaculum aerophilum with as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP core., Mura C, Cascio D, Sawaya MR, Eisenberg DS, Proc Natl Acad Sci U S A. 2001 May 8;98(10):5532-7. Epub 2001 May 1. PMID:11331747

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