|Protein Science (2007) 16(3):535-8|
|Northeast Structural Genomics Consortium|
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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.
|chemistry metabolism |
|Crystallography, X-Ray Models, Molecular Conserved Sequence Dimerization Membrane Transport Proteins Molecular Sequence Data Protein Conformation Sequence Alignment Oxidoreductases Agrobacterium tumefaciens Binding Sites Heme Oxygenase (Decyclizing) Amino Acid Sequence Bacterial Proteins |
|1 (Last update: 09/16/2017 11:12:53am)|
|Protein Sci. 2007 Mar;16(3):535-8.|