1m5q

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(New page: 200px<br /><applet load="1m5q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5q, resolution 2.00&Aring;" /> '''Crystal structure of...)
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'''Crystal structure of a novel Sm-like archaeal protein from Pyrobaculum aerophilum'''<br />
'''Crystal structure of a novel Sm-like archaeal protein from Pyrobaculum aerophilum'''<br />
==Overview==
==Overview==
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To better understand the roles of Sm proteins in forming the cores of many, RNA-processing ribonucleoproteins, we determined the crystal structure of, an atypical Sm-like archaeal protein (SmAP3) in which the conserved Sm, domain is augmented by a previously uncharacterized, mixed alpha/beta, C-terminal domain. The structure reveals an unexpected SmAP3 14-mer that, is perforated by a cylindrical pore and is bound to 14 cadmium (Cd(2+)), ions. Individual heptamers adopt either "apical" or "equatorial", conformations that chelate Cd(2+) differently. SmAP3 forms supraheptameric, oligomers (SmAP3)(n = 7,14,28) in solution, and assembly of the asymmetric, 14-mer is modulated by differential divalent cation-binding in apical and, equatorial subunits. Phylogenetic and sequence analyses substantiate, SmAP3s as a unique subset of SmAPs. These results distinguish SmAP3s from, other Sm proteins and provide a model for the structure and properties of, Sm proteins &gt;100 residues in length, e.g., several human Sm proteins.
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To better understand the roles of Sm proteins in forming the cores of many RNA-processing ribonucleoproteins, we determined the crystal structure of an atypical Sm-like archaeal protein (SmAP3) in which the conserved Sm domain is augmented by a previously uncharacterized, mixed alpha/beta C-terminal domain. The structure reveals an unexpected SmAP3 14-mer that is perforated by a cylindrical pore and is bound to 14 cadmium (Cd(2+)) ions. Individual heptamers adopt either "apical" or "equatorial" conformations that chelate Cd(2+) differently. SmAP3 forms supraheptameric oligomers (SmAP3)(n = 7,14,28) in solution, and assembly of the asymmetric 14-mer is modulated by differential divalent cation-binding in apical and equatorial subunits. Phylogenetic and sequence analyses substantiate SmAP3s as a unique subset of SmAPs. These results distinguish SmAP3s from other Sm proteins and provide a model for the structure and properties of Sm proteins &gt;100 residues in length, e.g., several human Sm proteins.
==About this Structure==
==About this Structure==
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1M5Q 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 CD, NA, GOL and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M5Q OCA].
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1M5Q 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=CD:'>CD</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5Q OCA].
==Reference==
==Reference==
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[[Category: ob-like fold]]
[[Category: ob-like fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:48:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:44 2008''

Revision as of 11:51, 21 February 2008

Image:1m5q.gif

1m5q, resolution 2.00Å

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Crystal structure of a novel Sm-like archaeal protein from Pyrobaculum aerophilum

Overview

To better understand the roles of Sm proteins in forming the cores of many RNA-processing ribonucleoproteins, we determined the crystal structure of an atypical Sm-like archaeal protein (SmAP3) in which the conserved Sm domain is augmented by a previously uncharacterized, mixed alpha/beta C-terminal domain. The structure reveals an unexpected SmAP3 14-mer that is perforated by a cylindrical pore and is bound to 14 cadmium (Cd(2+)) ions. Individual heptamers adopt either "apical" or "equatorial" conformations that chelate Cd(2+) differently. SmAP3 forms supraheptameric oligomers (SmAP3)(n = 7,14,28) in solution, and assembly of the asymmetric 14-mer is modulated by differential divalent cation-binding in apical and equatorial subunits. Phylogenetic and sequence analyses substantiate SmAP3s as a unique subset of SmAPs. These results distinguish SmAP3s from other Sm proteins and provide a model for the structure and properties of Sm proteins >100 residues in length, e.g., several human Sm proteins.

About this Structure

1M5Q is a Single protein structure of sequence from Pyrobaculum aerophilum with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure and assembly of an augmented Sm-like archaeal protein 14-mer., Mura C, Phillips M, Kozhukhovsky A, Eisenberg D, Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4539-44. Epub 2003 Mar 31. PMID:12668760

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