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      The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism

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      Acta Crystallographica Section F: Structural Biology and Crystallization Communications
      International Union of Crystallography
      Joint Center for Structural Genomics (JCSG) special issue
      structural genomics, DUFs, glycolipids, osmotic stress, host–pathogen interactions

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          Abstract

          PA1994, a Pfam PF06475 (DUF1089) family homolog from P. aeruginosa, reveals remote similarities to lipoprotein localization factors and a conserved putative glycolipid-binding site.

          Abstract

          The crystal structure of PA1994 from Pseudomonas aeruginosa, a member of the Pfam PF06475 family classified as a domain of unknown function (DUF1089), reveals a novel fold comprising a 15-stranded β-sheet wrapped around a single α-helix that assembles into a tight dimeric arrangement. The remote structural similarity to lipoprotein localization factors, in addition to the presence of an acidic pocket that is conserved in DUF1089 homologs, phospholipid-binding and sugar-binding proteins, indicate a role for PA1994 and the DUF1089 family in glycolipid metabolism. Genome-context analysis lends further support to the involvement of this family of proteins in glycolipid metabolism and indicates possible activation of DUF1089 homologs under conditions of bacterial cell-wall stress or host–pathogen interactions.

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          Author and article information

          Conference
          Acta Crystallogr Sect F Struct Biol Cryst Commun
          Acta Cryst. F
          Acta Crystallographica Section F: Structural Biology and Crystallization Communications
          International Union of Crystallography
          1744-3091
          1 October 2010
          27 October 2009
          27 October 2009
          : 66
          : Pt 10 ( publisher-idID: f101000 )
          : 1211-1217
          Affiliations
          [a ]Joint Center for Structural Genomics, http://www.jcsg.org, USA
          [b ]Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, CA, USA
          [c ]Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA
          [d ]Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, CA, USA
          [e ]Center for Research in Biological Systems, University of California, San Diego, La Jolla, CA, USA
          [f ]Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA, USA
          [g ]Département de Biochimie, Université de Sherbrooke, Québec, Canada
          [h ]Photon Science, SLAC National Accelerator Laboratory, Menlo Park, CA, USA
          Author notes
          Correspondence e-mail: wilson@ 123456scripps.edu
          Article
          wd5111 ACSFCL S1744309109022684
          10.1107/S1744309109022684
          2954207
          20944213
          8cb48d1b-82b4-4e9f-8fc4-fb8d8208fcfd
          © Bakolitsa et al. 2010

          This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

          Joint Center for Structural Genomics (JCSG) special issue
          History
          : 16 April 2009
          : 12 June 2009
          Categories
          New Folds

          Molecular biology
          host–pathogen interactions,osmotic stress,dufs,glycolipids,structural genomics
          Molecular biology
          host–pathogen interactions, osmotic stress, dufs, glycolipids, structural genomics

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