2ph0
Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.
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OverviewOverview
We report here the crystal structure at 2.0 A 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.
About this StructureAbout this Structure
2PH0 is a Single protein structure of sequence from Pectobacterium carotovorum. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of AGR_C_4470p from Agrobacterium tumefaciens., Vorobiev SM, Neely H, Seetharaman J, Ma LC, Xiao R, Acton TB, Montelione GT, Tong L, Protein Sci. 2007 Mar;16(3):535-8. PMID:17322535
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