2ph0

Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.

spinqualitylabelsall models 2ph0, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ph0 is a 2 chain structure with sequence from "bacillus_carotovorus"_jones_1901 "bacillus carotovorus" jones 1901. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Related: 2ovi, 2hqv Gene: ECA3008 ("Bacillus carotovorus" Jones 1901) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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