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The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism
- Bakolitsa, Constantina;
- Kumar, Abhinav;
- McMullan, Daniel;
- Krishna, S Sri;
- Miller, Mitchell D;
- Carlton, Dennis;
- Najmanovich, Rafael;
- Abdubek, Polat;
- Astakhova, Tamara;
- Chiu, Hsiu-Ju;
- Clayton, Thomas;
- Deller, Marc C;
- Duan, Lian;
- Elias, Ylva;
- Feuerhelm, Julie;
- Grant, Joanna C;
- Grzechnik, Slawomir K;
- Han, Gye Won;
- Jaroszewski, Lukasz;
- Jin, Kevin K;
- Klock, Heath E;
- Knuth, Mark W;
- Kozbial, Piotr;
- Marciano, David;
- Morse, Andrew T;
- Nigoghossian, Edward;
- Okach, Linda;
- Oommachen, Silvya;
- Paulsen, Jessica;
- Reyes, Ron;
- Rife, Christopher L;
- Trout, Christina V;
- van den Bedem, Henry;
- Weekes, Dana;
- White, Aprilfawn;
- Xu, Qingping;
- Hodgson, Keith O;
- Wooley, John;
- Elsliger, Marc-André;
- Deacon, Ashley M;
- Godzik, Adam;
- Lesley, Scott A;
- Wilson, Ian A
- et al.
Published Web Location
https://doi.org/10.1107/s1744309109022684Abstract
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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