Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism

Constantina Bakolitsa, Abhinav Kumar, Kevin K. Jin, Daniel McMullan, S. Sri Krishna, Mitchell D. Miller, Polat Abdubek, Claire Acosta, Tamara Astakhova, Herbert L. Axelrod, Prasad Burra, Dennis Carlton, Connie Chen, Hsiu Ju Chiu, Thomas Clayton, Debanu Das, Marc C. Deller, Lian Duan, Ylva Elias, Kyle EllrottDustin Ernst, Carol L. Farr, Julie Feuerhelm, Joanna C. Grant, Anna Grzechnik, Slawomir K. Grzechnik, Gye Won Han, Lukasz Jaroszewski, Hope A. Johnson, Heath E. Klock, Mark W. Knuth, Piotr Kozbial, David Marciano, Andrew T. Morse, Kevin D. Murphy, Edward Nigoghossian, Amanda Nopakun, Linda Okach, Jessica Paulsen, Christina Puckett, Ron Reyes, Christopher L. Rife, Natasha Sefcovic, Henry J. Tien, Christine B. Trame, Christina V. Trout, Henry Van Den Bedem, Dana Weekes, Aprilfawn White, Qingping Xu, Keith O. Hodgson, John Wooley, Marc Andre Elsliger, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 Å by single-wavelength anomalous dispersion and multiple-wavelength anomalous dispersion, respectively, using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). These proteins are the first structural representatives of the PF06684 (DUF1185) Pfam family. Structural analysis revealed that both structures adopt a variant of the Bacillus chorismate mutase fold (BCM). The biological unit of both proteins is a hexamer and analysis of homologs indicates that the oligomer interface residues are highly conserved. The conformation of the critical regions for oligomerization appears to be dependent on pH or salt concentration, suggesting that this protein might be subject to environmental regulation. Structural similarities to BCM and genome-context analysis suggest a function in amino-acid synthesis.

Original languageEnglish (US)
Pages (from-to)1182-1189
Number of pages8
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number10
DOIs
StatePublished - Oct 1 2010

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Keywords

  • amino acids
  • chorismate mutase
  • domain of unknown function
  • pH-dependent
  • salt-dependent
  • structural genomics

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Cite this

Bakolitsa, C., Kumar, A., Jin, K. K., McMullan, D., Krishna, S. S., Miller, M. D., Abdubek, P., Acosta, C., Astakhova, T., Axelrod, H. L., Burra, P., Carlton, D., Chen, C., Chiu, H. J., Clayton, T., Das, D., Deller, M. C., Duan, L., Elias, Y., ... Wilson, I. A. (2010). Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(10), 1182-1189. https://doi.org/10.1107/S1744309109050647