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1m5q
From Proteopedia
(New page: 200px<br /><applet load="1m5q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5q, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1m5q.gif|left|200px]]<br /><applet load="1m5q" size=" | + | [[Image:1m5q.gif|left|200px]]<br /><applet load="1m5q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m5q, resolution 2.00Å" /> | caption="1m5q, resolution 2.00Å" /> | ||
'''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== | ||
| - | To better understand the roles of Sm proteins in forming the cores of many | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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]] | ||
| - | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 13:51:44 2008
Categories: Pyrobaculum aerophilum | Single protein | Eisenberg, D. | Kozhukhovsky, A. | Mura, C. | Phillips, M. | ACY | CD | GOL | NA | 14-mer | B-sheet toroid | Cadmium-binding site | Ob-like fold
