| Literature DB >> 19173316 |
Debanu Das1, Piotr Kozbial, Herbert L Axelrod, Mitchell D Miller, Daniel McMullan, S Sri Krishna, Polat Abdubek, Claire Acosta, Tamara Astakhova, Prasad Burra, Dennis Carlton, Connie Chen, Hsiu-Ju Chiu, Thomas Clayton, Marc C Deller, Lian Duan, Ylva Elias, Marc-André Elsliger, Dustin Ernst, Carol Farr, Julie Feuerhelm, Anna Grzechnik, Slawomir K Grzechnik, Joanna Hale, Gye Won Han, Lukasz Jaroszewski, Kevin K Jin, Hope A Johnson, Heath E Klock, Mark W Knuth, Abhinav Kumar, David Marciano, Andrew T Morse, Kevin D Murphy, Edward Nigoghossian, Amanda Nopakun, Linda Okach, Silvya Oommachen, Jessica Paulsen, Christina Puckett, Ron Reyes, Christopher L Rife, Natasha Sefcovic, Sebastian Sudek, Henry Tien, Christine Trame, Christina V Trout, Henry van den Bedem, Dana Weekes, Aprilfawn White, Qingping Xu, Keith O Hodgson, John Wooley, Ashley M Deacon, Adam Godzik, Scott A Lesley, Ian A Wilson.
Abstract
ECX21941 represents a very large family (over 600 members) of novel, ocean metagenome-specific proteins identified by clustering of the dataset from the Global Ocean Sampling expedition. The crystal structure of ECX21941 reveals unexpected similarity to Sm/LSm proteins, which are important RNA-binding proteins, despite no detectable sequence similarity. The ECX21941 protein assembles as a homopentamer in solution and in the crystal structure when expressed in Escherichia coli and represents the first pentameric structure for this Sm/LSm family of proteins, although the actual oligomeric form in vivo is currently not known. The genomic neighborhood analysis of ECX21941 and its homologs combined with sequence similarity searches suggest a cyanophage origin for this protein. The specific functions of members of this family are unknown, but our structure analysis of ECX21941 indicates nucleic acid-binding capabilities and suggests a role in RNA and/or DNA processing.Entities:
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Year: 2009 PMID： 19173316 PMCID： PMC2785455 DOI： 10.1002/prot.22360
Source DB: PubMed Journal: Proteins ISSN： 0887-3585