Open and closed conformations of two SpoIIAA-like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand binding
dc.contributor.author | Kumar, Abhinav | en_US |
dc.contributor.author | Lomize, Andrei L. | en_US |
dc.contributor.author | Jin, Kevin K. | en_US |
dc.contributor.author | Carlton, Dennis | en_US |
dc.contributor.author | Miller, Mitchell D. | en_US |
dc.contributor.author | Jaroszewski, Lukasz | en_US |
dc.contributor.author | Abdubek, Polat | en_US |
dc.contributor.author | Astakhova, Tamara | en_US |
dc.contributor.author | Axelrod, Herbert L. | en_US |
dc.contributor.author | Chiu, Hsiu-Ju | en_US |
dc.contributor.author | Clayton, Thomas | en_US |
dc.contributor.author | Das, Debanu | en_US |
dc.contributor.author | Deller, Marc C. | en_US |
dc.contributor.author | Duan, Lian | en_US |
dc.contributor.author | Feuerhelm, Julie | en_US |
dc.contributor.author | Grant, Joanna C. | en_US |
dc.contributor.author | Grzechnik, Anna | en_US |
dc.contributor.author | Han, Gye Won | en_US |
dc.contributor.author | Klock, Heath E. | en_US |
dc.contributor.author | Knuth, Mark W. | en_US |
dc.contributor.author | Kozbial, Piotr | en_US |
dc.contributor.author | Krishna, S. Sri | en_US |
dc.contributor.author | Marciano, David | en_US |
dc.contributor.author | Mcmullan, Daniel | en_US |
dc.contributor.author | Morse, Andrew T. | en_US |
dc.contributor.author | Nigoghossian, Edward | en_US |
dc.contributor.author | Okach, Linda | en_US |
dc.contributor.author | Reyes, Ron | en_US |
dc.contributor.author | Rife, Christopher L. | en_US |
dc.contributor.author | Sefcovic, Natasha | en_US |
dc.contributor.author | Tien, Henry J. | en_US |
dc.contributor.author | Trame, Christine B. | en_US |
dc.contributor.author | Van Den Bedem, Henry | en_US |
dc.contributor.author | Weekes, Dana | en_US |
dc.contributor.author | Xu, Qingping | en_US |
dc.contributor.author | Hodgson, Keith O. | en_US |
dc.contributor.author | Wooley, John | en_US |
dc.contributor.author | Elsliger, Marc-André | en_US |
dc.contributor.author | Deacon, Ashley M. | en_US |
dc.contributor.author | Godzik, Adam | en_US |
dc.contributor.author | Lesley, Scott A. | en_US |
dc.contributor.author | Wilson, Ian A. | en_US |
dc.date.accessioned | 2011-01-31T18:01:39Z | |
dc.date.available | 2011-12-02T15:41:52Z | en_US |
dc.date.issued | 2010-10-01 | en_US |
dc.identifier.citation | Kumar, Abhinav; Lomize, Andrei; Jin, Kevin K.; Carlton, Dennis; Miller, Mitchell D.; Jaroszewski, Lukasz; Abdubek, Polat; Astakhova, Tamara; Axelrod, Herbert L.; Chiu, Hsiu-Ju; 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, Marc-André; Deacon, Ashley M.; Godzik, Adam; Lesley, Scott A.; Wilson, Ian A.; (2010). "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 Crystallographica Section F 66(10): 1245-1253. <http://hdl.handle.net/2027.42/79393> | en_US |
dc.identifier.issn | 1744-3091 | en_US |
dc.identifier.issn | 1744-3091 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/79393 | |
dc.description.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 14Å 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 14Å 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. | en_US |
dc.format.extent | 1178719 bytes | |
dc.format.extent | 3106 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | International Union of Crystallography | en_US |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.subject.other | YP_001095227.1 | en_US |
dc.subject.other | YP_749275.1 | en_US |
dc.subject.other | SpoIIAA-like Proteins | en_US |
dc.title | Open and closed conformations of two SpoIIAA-like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand binding | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationother | Joint Center for Structural Genomics, http://www.jcsg.org , USA | en_US |
dc.contributor.affiliationother | Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA | en_US |
dc.contributor.affiliationother | Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA, USA | en_US |
dc.contributor.affiliationother | Center for Research in Biological Systems, University of California, San Diego, La Jolla, CA, USA | en_US |
dc.contributor.affiliationother | Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, CA, USA | en_US |
dc.contributor.affiliationother | Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, CA, USA | en_US |
dc.contributor.affiliationother | Photon Science, SLAC National Accelerator Laboratory, Menlo Park, CA, USA | en_US |
dc.identifier.pmid | 20944218 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/79393/1/S1744309109042481.pdf | |
dc.identifier.doi | 10.1107/S1744309109042481 | en_US |
dc.identifier.source | Acta Crystallographica Section F | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.