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Open and closed conformations of two SpoIIAA‐like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand binding
Author(s) -
Kumar Abhinav,
Lomize Andrei,
Jin Kevin K.,
Carlton Dennis,
Miller Mitchell D.,
Jaroszewski Lukasz,
Abdubek Polat,
Astakhova Tamara,
Axelrod Herbert L.,
Chiu HsiuJu,
Clayton Thomas,
Das Debanu,
Deller Marc C.,
Duan Lian,
Feuerhelm Julie,
Grant Joanna C.,
Grzechnik Anna,
Han Gye Won,
Klock Heath E.,
Knuth Mark W.,
Kozbial Piotr,
Krishna S. Sri,
Marciano David,
McMullan Daniel,
Morse Andrew T.,
Nigoghossian Edward,
Okach Linda,
Reyes Ron,
Rife Christopher L.,
Sefcovic Natasha,
Tien Henry J.,
Trame Christine B.,
Van Den Bedem Henry,
Weekes Dana,
Xu Qingping,
Hodgson Keith O.,
Wooley John,
Elsliger MarcAndré,
Deacon Ashley M.,
Godzik Adam,
Lesley Scott A.,
Wilson Ian A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109042481
Subject(s) - amphiphile , lipid bilayer , chemistry , bilayer , crystallography , monomer , model lipid bilayer , membrane protein , biophysics , stereochemistry , membrane , biochemistry , lipid bilayer phase behavior , biology , polymer , organic chemistry , copolymer
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 α/β 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 α2 and α3 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, α2 and α3, into the lipid bilayer. These bacterial proteins may function as carriers of nonpolar substances or as interfacially activated enzymes.

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