Crystal structure of AGR_C_4470p from Agrobacterium tumefaciens

Sergey M. Vorobiev, Helen Neely, Jayaraman Seetharaman, Li Chung Ma, Rong Xiao, Thomas B. Acton, Gaetano T. Montelione, Liang Tong

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


We report here the crystal structure at 2.0 Å resolution of the AGR_C_4470p protein from the Gram-negative bacterium Agrobacterium tumefaciens. The protein is a tightly associated dimer, each subunit of which bears strong structural homology with the two domains of the heme utilization protein ChuS from Escherichia coli and HemS from Yersinia enterocolitica. Remarkably, the organization of the AGR_C_4470p dimer is the same as that of the two domains in ChuS and HemS, providing structural evidence that these two proteins evolved by gene duplication. However, the binding site for heme, while conserved in HemS and ChuS, is not conserved in AGR_C_4470p, suggesting that it probably has a different function. This is supported by the presence of two homologs of AGR_C_4470p in E. coli, in addition to the ChuS protein. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)535-538
Number of pages4
JournalProtein Science
Issue number3
StatePublished - Mar 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


  • ChuS
  • Gene duplication
  • HemS
  • Heme utilization enzyme
  • Molecular evolution
  • Protein structure
  • Structural genomics


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