5cl2
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cl2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5CL2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5cl2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5CL2 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5cl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cl2 OCA], [https://pdbe.org/5cl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cl2 RCSB], [https://www.ebi.ac.uk/pdbsum/5cl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cl2 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cl2 OCA], [https://pdbe.org/5cl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cl2 RCSB], [https://www.ebi.ac.uk/pdbsum/5cl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cl2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://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> | [https://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. | ||
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| - | 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> | ||
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| - | 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 == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of Spo0M, sporulation control protein, from Bacillus subtilis.
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