5cl2: Difference between revisions
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''' | ==Crystal structure of Spo0M, sporulation control protein, from Bacillus subtilis.== | ||
<StructureSection load='5cl2' size='340' side='right' caption='[[5cl2]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5cl2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CL2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cl2 OCA], [http://pdbe.org/5cl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cl2 RCSB], [http://www.ebi.ac.uk/pdbsum/5cl2 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SP0M_BACSU SP0M_BACSU]] Controls the expression of spo0A and is required to pass the morphological stage 0 of sporulation.<ref>PMID:9795118</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Spo0M is a sporulation-control protein that is thought to play an essential role in the early stage of endospore formation. While little is known about the functions of Spo0M, a recent phylogenetic study suggests that, based on its amino-acid sequence, Spo0M might belong to the arrestin clan. The crystal structure of the Spo0M protein was determined at a resolution of 2.3 A. Ten amino acids at the end of the N-terminus were removed to improve the thermal stability of the purified Spo0M protein and the crystal structure of Spo0M was determined by SAD. Spo0M has a well conserved N-terminal domain with an arrestin-like fold, which consists of a beta-strand sandwich structure. Surprisingly, the C-terminal domain of Spo0M, which has no structural homology to arrestin-clan proteins, bears significant structural similarity to the FP domain of the human PI31 protein. In addition, Spo0M harbours a potential polar-core structure connecting the N- and C-terminal domains with several salt bridges, as seen in the crystal structures of arrestin and VPS26. The structure reported here constitutes the first structural information on a bacterial protein that shares significant structural homology to members of the arrestin clan and the FP domain. | |||
Structure of Spo0M, a sporulation-control protein from Bacillus subtilis.,Sonoda Y, Mizutani K, Mikami B Acta Crystallogr F Struct Biol Commun. 2015 Dec 1;71(Pt 12):1488-97. doi:, 10.1107/S2053230X15020919. Epub 2015 Nov 18. PMID:26625291<ref>PMID:26625291</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5cl2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mikami, B]] | [[Category: Mikami, B]] | ||
[[Category: Mizutani, K]] | |||
[[Category: Sonoda, Y]] | [[Category: Sonoda, Y]] | ||
[[Category: | [[Category: Protein binding]] | ||
[[Category: Spo0m]] | |||
[[Category: Sporulation]] | |||
Revision as of 13:52, 16 December 2015
Crystal structure of Spo0M, sporulation control protein, from Bacillus subtilis.
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