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Structures of the first representatives of Pfam family PF06938 (DUF1285) reveal a new fold with repeated structural motifs and possible involvement in signal transduction
- Han, Gye Won;
- Bakolitsa, Constantina;
- Miller, Mitchell D;
- Kumar, Abhinav;
- Carlton, Dennis;
- Najmanovich, Rafael J;
- Abdubek, Polat;
- Astakhova, Tamara;
- Axelrod, Herbert L;
- Chen, Connie;
- Chiu, Hsiu-Ju;
- Clayton, Thomas;
- Das, Debanu;
- Deller, Marc C;
- Duan, Lian;
- Ernst, Dustin;
- Feuerhelm, Julie;
- Grant, Joanna C;
- Grzechnik, Anna;
- Jaroszewski, Lukasz;
- Jin, Kevin K;
- Johnson, Hope A;
- 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
- et al.
Published Web Location
https://doi.org/10.1107/s1744309109050416Abstract
The crystal structures of SPO0140 and Sbal_2486 were determined using the semiautomated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). The structures revealed a conserved core with domain duplication and a superficial similarity of the C-terminal domain to pleckstrin homology-like folds. The conservation of the domain interface indicates a potential binding site that is likely to involve a nucleotide-based ligand, with genome-context and gene-fusion analyses additionally supporting a role for this family in signal transduction, possibly during oxidative stress.
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