Skip to main content
eScholarship
Open Access Publications from the University of California

UC Riverside

UC Riverside Previously Published Works bannerUC Riverside

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.

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

Many UC-authored scholarly publications are freely available on this site because of the UC's open access policies. Let us know how this access is important for you.

Main Content
Current View