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6bg8
From Proteopedia
(Difference between revisions)
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<StructureSection load='6bg8' size='340' side='right' caption='[[6bg8]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='6bg8' size='340' side='right' caption='[[6bg8]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6bg8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BG8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BG8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bg8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Shefn Shefn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BG8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BG8 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sfri_1018 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318167 SHEFN])</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=6bg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bg8 OCA], [http://pdbe.org/6bg8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bg8 RCSB], [http://www.ebi.ac.uk/pdbsum/6bg8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bg8 ProSAT]</span></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=6bg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bg8 OCA], [http://pdbe.org/6bg8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bg8 RCSB], [http://www.ebi.ac.uk/pdbsum/6bg8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bg8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Out of the dozen different ice-binding protein (IBP) structures known, the DUF3494 domain is the most widespread, having been passed many times between prokaryotic and eukaryotic microorganisms by horizontal gene transfer. This ~25-kDa beta-solenoid domain with an adjacent parallel alpha-helix is most commonly associated with an N-terminal secretory signal peptide. However, examples of the DUF3494 domain preceded by tandem Bacterial Immunoglobulin-like (BIg) domains are sometimes found, though uncharacterized. Here we present one such protein (SfIBP_1) from the Antarctic bacterium Shewanella frigidimarina. We have confirmed and characterized the ice-binding activity of its ice-binding domain using thermal hysteresis measurements, fluorescent ice plane affinity analysis, and ice recrystallization inhibition assays. X-ray crystallography was used to solve the structure of the SfIBP_1 ice-binding domain, to further characterize its ice-binding surface and unique method of stabilizing or "capping" the ends of the solenoid structure. The latter is formed from the interaction of two loops mediated by a combination of tandem prolines and electrostatic interactions. Furthermore, given their domain architecture and membrane association, we propose that these BIg-containing DUF3494 IBPs serve as ice-binding adhesion proteins that are capable of adsorbing their host bacterium onto ice. This article is protected by copyright. All rights reserved. | ||
| + | |||
| + | An ice-binding and tandem beta-sandwich domain-containing protein in Shewanella frigidimarina is a potential new type of ice adhesin.,Vance TDR, Graham LA, Davies PL FEBS J. 2018 Mar 2. doi: 10.1111/febs.14424. PMID:29498209<ref>PMID:29498209</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6bg8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Shefn]] | ||
[[Category: Davies, P L]] | [[Category: Davies, P L]] | ||
[[Category: Vance, T D.R]] | [[Category: Vance, T D.R]] | ||
Revision as of 07:01, 14 March 2018
Shewanella frigidimarina ice-binding protein_1 DUF3494 Domain
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