2OOK

Crystal structure of a protein with unknown function (YP_749275.1) from Shewanella Frigidimarina NCIMB 400 at 1.80 A resolution

Summary for 2OOK

• Entry DOI: 10.2210/pdb2ook/pdb
• Descriptor: Hypothetical protein, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: yp_749275.1, hypothetical protein, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, unknown function
• Biological source: Shewanella frigidimarina
• Total number of polymer chains: 2
• Total formula weight: 29809.06

Authors

Joint Center for Structural Genomics (JCSG) (deposition date: 2007-01-25, release date: 2007-02-06, Last modification date: 2024-11-13)

Primary citation

Kumar, A.,Lomize, A.,Jin, K.K.,Carlton, D.,Miller, M.D.,Jaroszewski, L.,Abdubek, P.,Astakhova, T.,Axelrod, H.L.,Chiu, H.J.,Clayton, T.,Das, D.,Deller, M.C.,Duan, L.,Feuerhelm, J.,Grant, J.C.,Grzechnik, A.,Han, G.W.,Klock, H.E.,Knuth, M.W.,Kozbial, P.,Krishna, S.S.,Marciano, D.,McMullan, D.,Morse, A.T.,Nigoghossian, E.,Okach, L.,Reyes, R.,Rife, C.L.,Sefcovic, N.,Tien, H.J.,Trame, C.B.,van den Bedem, H.,Weekes, D.,Xu, Q.,Hodgson, K.O.,Wooley, J.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A.
Open and closed conformations of two SpoIIAA-like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand binding.
Acta Crystallogr.,Sect.F, 66:1245-1253, 2010

PubMed Abstract: 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.

PubMed: 20944218
DOI: 10.1107/S1744309109042481

Experimental method

X-RAY DIFFRACTION (1.8 Å)