1m5q

<table><tr><td colspan='2'>[[1m5q]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51768 Atcc 51768]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1M5Q FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1i8f|1i8f]], [[1jbm|1jbm]], [[1i4k|1i4k]], [[1d3b|1d3b]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SmAP3 gene (Pae2122) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 ATCC 51768])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1m5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5q OCA], [http://pdbe.org/1m5q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m5q RCSB], [http://www.ebi.ac.uk/pdbsum/1m5q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5q ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12668760</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1m5q" style="background-color:#fffaf0;"></div>

*[[Sm-like protein|Sm-like protein]]

[[Category: Atcc 51768]]

[[Category: Eisenberg, D]]

[[Category: Kozhukhovsky, A]]

[[Category: Mura, C]]

[[Category: Phillips, M]]

[[Category: Translation]]