Genomics, evolution, and crystal structure of a new family of bacterial spore kinases

Scheeff, Eric D.; Axelrod, Herbert L.; Miller, Mitchell D.; Chiu, Hsiu-Ju; Deacon, Ashley M.; Wilson, Ian A.; Manning, Gerard

doi:10.1002/prot.22663

Title: Genomics, evolution, and crystal structure of a new family of bacterial spore kinases

Journal Article · 24 November 2009 · Proteins

DOI: https://doi.org/10.1002/prot.22663 · OSTI ID:1623589

Scheeff, Eric D. ^[1]; Axelrod, Herbert L. ^[2]; Miller, Mitchell D. ^[2]; Chiu, Hsiu-Ju ^[2]; Deacon, Ashley M. ^[2]; Wilson, Ian A. ^[3]; Manning, Gerard ^[4]

Salk Inst. for Biological Studies, La Jolla, CA (United States). Razavi Newman Center for Bioinformatics; DOE/OSTI
Joint Center for Structrual Genomics (JCSG), San Diego, CA (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Joint Center for Structrual Genomics (JCSG), San Diego, CA (United States); The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology
Salk Inst. for Biological Studies, La Jolla, CA (United States). Razavi Newman Center for Bioinformatics

Bacterial spore formation is a complex process of fundamental relevance to biology and human disease. The spore coat structure is complex and poorly understood, and the roles of many of the protein components remain unclear. We describe a new family of spore coat proteins, the bacterial spore kinases (BSKs), and the first crystal structure of a BSK, YtaA (CotI) from Bacillus subtilis. BSKs are widely distributed in spore-forming Bacillus and Clostridium species, and have a dynamic evolutionary history. Sequence and structure analyses indicate that the BSKs are CAKs, a prevalent group of small molecule kinases in bacteria that is distantly related to the eukaryotic protein kinases. YtaA has substantial structural similarity to CAKs, but also displays distinctive features that broaden our understanding of the CAK group. Evolutionary constraint analysis of the protein surfaces indicates that members of the BSK family have distinct clade-conserved patterns in the substrate binding region, and probably bind and phosphorylate distinct targets. Several classes of BSKs have apparently independently lost catalytic activity to become pseudokinases, indicating that the family also has a major noncatalytic function.

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Research Organization:: SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1623589

Journal Information:: Proteins, Journal Name: Proteins Journal Issue: 6 Vol. 78; ISSN 0887-3585

Publisher:: WileyCopyright Statement

Country of Publication:: United States

Language:: English

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