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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 10
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pubmed:dateCreated |
2010-10-14
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pubmed:databankReference |
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pubmed:abstractText |
The crystal structures of the proteins encoded by the YP_749275.1 and YP_001095227.1 genes from Shewanella frigidimarina and S. loihica, respectively, have been determined at 1.8 and 2.25?Å resolution, respectively. These proteins are members of a novel family of bacterial proteins that adopt the ?/? SpoIIAA-like fold found in STAS and CRAL-TRIO domains. Despite sharing 54% sequence identity, these two proteins adopt distinct conformations arising from different dispositions of their ?2 and ?3 helices. In the `open' conformation (YP_001095227.1), these helices are 15?Å apart, leading to the creation of a deep nonpolar cavity. In the `closed' structure (YP_749275.1), the helices partially unfold and rearrange, occluding the cavity and decreasing the solvent-exposed hydrophobic surface. These two complementary structures are reminiscent of the conformational switch in CRAL-TRIO carriers of hydrophobic compounds. It is suggested that both proteins may associate with the lipid bilayer in their `open' monomeric state by inserting their amphiphilic helices, ?2 and ?3, into the lipid bilayer. These bacterial proteins may function as carriers of nonpolar substances or as interfacially activated enzymes.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1744-3091
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pubmed:author |
pubmed-author:AbdubekPolatP,
pubmed-author:AstakhovaTamaraT,
pubmed-author:AxelrodHerbert LHL,
pubmed-author:CarltonDennisD,
pubmed-author:ChiuHsiu JuHJ,
pubmed-author:DasDebanuD,
pubmed-author:DeaconAshley MAM,
pubmed-author:DellerMarc CMC,
pubmed-author:DuanLianL,
pubmed-author:ElsligerMarc AndréMA,
pubmed-author:FeuerhelmJulieJ,
pubmed-author:GodzikAdamA,
pubmed-author:GrantJoanna CJC,
pubmed-author:GrzechnikAnnaA,
pubmed-author:HanGye WonGW,
pubmed-author:HodgsonKeith OKO,
pubmed-author:JaroszewskiLukaszL,
pubmed-author:JinKevin KKK,
pubmed-author:KlockHeath EHE,
pubmed-author:KnuthMark WMW,
pubmed-author:KozbialPiotrP,
pubmed-author:KrishnaS SriSS,
pubmed-author:KumarAbhinavA,
pubmed-author:LesleyScott ASA,
pubmed-author:LomizeAndreiA,
pubmed-author:MarcianoDavidD,
pubmed-author:McMullanDanielD,
pubmed-author:MillerMitchell DMD,
pubmed-author:MorseAndrew TAT,
pubmed-author:NigoghossianEdwardE,
pubmed-author:OkachLindaL,
pubmed-author:ReyesRonR,
pubmed-author:RifeChristopher LCL,
pubmed-author:SefcovicNatashaN,
pubmed-author:ThomasClaytonC,
pubmed-author:TienHenry JHJ,
pubmed-author:TrameChristine BCB,
pubmed-author:WeekesDanaD,
pubmed-author:WilsonIan AIA,
pubmed-author:WooleyJohnJ,
pubmed-author:XuQingpingQ,
pubmed-author:van den BedemHenryH
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1245-53
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pubmed:meshHeading |
pubmed-meshheading:20944218-Amino Acid Sequence,
pubmed-meshheading:20944218-Bacterial Proteins,
pubmed-meshheading:20944218-Cell Membrane,
pubmed-meshheading:20944218-Crystallography, X-Ray,
pubmed-meshheading:20944218-Ligands,
pubmed-meshheading:20944218-Models, Molecular,
pubmed-meshheading:20944218-Molecular Sequence Data,
pubmed-meshheading:20944218-Protein Binding,
pubmed-meshheading:20944218-Protein Structure, Quaternary,
pubmed-meshheading:20944218-Protein Structure, Tertiary,
pubmed-meshheading:20944218-Sequence Alignment,
pubmed-meshheading:20944218-Sequence Homology, Amino Acid,
pubmed-meshheading:20944218-Shewanella,
pubmed-meshheading:20944218-Structural Homology, Protein
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pubmed:year |
2010
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pubmed:articleTitle |
Open and closed conformations of two SpoIIAA-like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand binding.
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pubmed:affiliation |
Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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