Structural and Sequence Analysis of Imelysin-Like Proteins Implicated in Bacterial Iron Uptake

Xu, Qingping; Rawlings, Neil D.; Farr, Carol L.; Chiu, Hsiu-Ju; Grant, Joanna C.; Jaroszewski, Lukasz; Klock, Heath E.; Knuth, Mark W.; Miller, Mitchell D.; Weekes, Dana; Elsliger, Marc-André; Deacon, Ashley M.; Godzik, Adam; Lesley, Scott A.; Wilson, Ian A.

doi:10.1371/journal.pone.0021875

Structural and Sequence Analysis of Imelysin-Like Proteins Implicated in Bacterial Iron Uptake

Journal Article · Mon Jul 25 00:00:00 EDT 2011 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0021875· OSTI ID:1627465

Xu, Qingping ^[1]; Rawlings, Neil D. ^[2]; Farr, Carol L. ^[3]; Chiu, Hsiu-Ju ^[4]; Grant, Joanna C. ^[5]; Jaroszewski, Lukasz ^[6]; Klock, Heath E. ^[5]; Knuth, Mark W. ^[5]; Miller, Mitchell D. ^[4]; Weekes, Dana ^[7]; Elsliger, Marc-André ^[3]; Deacon, Ashley M. ^[4]; Godzik, Adam ^[6]; Lesley, Scott A. ^[8]; Wilson, Ian A. ^[3]

Joint Center for Structural Genomics, La Jolla, CA (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL); DOE/OSTI
Wellcome Trust Sanger Inst., Hinxton (United States)
Joint Center for Structural Genomics, La Jolla, CA (United States); The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology
Joint Center for Structural Genomics, La Jolla, CA (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Joint Center for Structural Genomics, La Jolla, CA (United States); Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.
Joint Center for Structural Genomics, La Jolla, CA (United States); Univ. of California, San Diego, La Jolla, CA (United States). Center for Research in Biological Systems; Sanford-Burnham Medical Research Institute, La Jolla, CA (United States). Program on Bioinformatics and Systems Biology
Joint Center for Structural Genomics, La Jolla, CA (United States); Sanford-Burnham Medical Research Institute, La Jolla, CA (United States). Program on Bioinformatics and Systems Biology
Joint Center for Structural Genomics, La Jolla, CA (United States); The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology; Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.

Imelysin-like proteins define a superfamily of bacterial proteins that are likely involved in iron uptake. Members of this superfamily were previously thought to be peptidases and were included in the MEROPS family M75. We determined the first crystal structures of two remotely related, imelysin-like proteins. The Psychrobacter arcticus structure was determined at 2.15 Å resolution and contains the canonical imelysin fold, while higher resolution structures from the gut bacteria Bacteroides ovatus, in two crystal forms (at 1.25 Å and 1.44 Å resolution), have a circularly permuted topology. Both structures are highly similar to each other despite low sequence similarity and circular permutation. The all-helical structure can be divided into two similar four-helix bundle domains. The overall structure and the GxHxxE motif region differ from known HxxE metallopeptidases, suggesting that imelysin-like proteins are not peptidases. A putative functional site is located at the domain interface. We have now organized the known homologous proteins into a superfamily, which can be separated into four families. These families share a similar functional site, but each has family-specific structural and sequence features. These results indicate that imelysin-like proteins have evolved from a common ancestor, and likely have a conserved function.

View Accepted Manuscript (DOE)

Research Organization:: SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); National Institute of General Medical Sciences (NIGMS); USDOE Office of Science (SC), Basic Energy Sciences (BES); National Center for Research Resources (NCRR)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1627465

Journal Information:: PLoS ONE, Journal Name: PLoS ONE Journal Issue: 7 Vol. 6; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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Structural and Sequence Analysis of Imelysin-Like Proteins Implicated in Bacterial Iron Uptake

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References (45)

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