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Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino‐acid metabolism
- Bakolitsa, Constantina;
- Kumar, Abhinav;
- Carlton, Dennis;
- Miller, Mitchell D;
- Krishna, S Sri;
- Abdubek, Polat;
- Astakhova, Tamara;
- Axelrod, Herbert L;
- Chiu, Hsiu-Ju;
- Clayton, Thomas;
- Deller, Marc C;
- Duan, Lian;
- Elsliger, Marc-André;
- Feuerhelm, Julie;
- Grzechnik, Slawomir K;
- Grant, Joanna C;
- Han, Gye Won;
- Jaroszewski, Lukasz;
- Jin, Kevin K;
- Klock, Heath E;
- Knuth, Mark W;
- Kozbial, Piotr;
- Marciano, David;
- McMullan, Daniel;
- Morse, Andrew T;
- Nigoghossian, Edward;
- Okach, Linda;
- Oommachen, Silvya;
- Paulsen, Jessica;
- Reyes, Ron;
- Rife, Christopher L;
- Tien, Henry J;
- Trout, Christina V;
- van den Bedem, Henry;
- Weekes, Dana;
- Xu, Qingping;
- Hodgson, Keith O;
- Wooley, John;
- Deacon, Ashley M;
- Godzik, Adam;
- Lesley, Scott A;
- Wilson, Ian A
- et al.
Published Web Location
https://doi.org/10.1107/s1744309109023689Abstract
The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel α+β fold comprising two β-sheets packed against a single helix. A remote structural similarity to two other uncharacterized protein families specific to the Bacillus genus (PF08868 and PF08968), as well as to prokaryotic S-adenosylmethionine decarboxylases, is consistent with a role in amino-acid metabolism. Genomic neighborhood analysis of LP2179 supports this functional assignment, which might also then be extended to PF08868 and PF08968.
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