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Title: Crystal Structure of AGR_C_4470p from Agrobacterium tumefaciens

Abstract

We report here the crystal structure at 2.0 {angstrom} 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.

Authors:
; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930404
Report Number(s):
BNL-81131-2008-JA
Journal ID: ISSN 0961-8368; TRN: US200904%%684
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Protein Science; Journal Volume: 16
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; BACTERIA; CRYSTAL STRUCTURE; DIMERS; ESCHERICHIA COLI; GENES; HEME; PROTEINS; national synchrotron light source

Citation Formats

Vorobiev,S., Neely, H., Seetharaman, J., Ma, L., Xiao, R., Acton, T., Montelione, G., and Tong, L. Crystal Structure of AGR_C_4470p from Agrobacterium tumefaciens. United States: N. p., 2007. Web. doi:10.1110/ps.062663307.
Vorobiev,S., Neely, H., Seetharaman, J., Ma, L., Xiao, R., Acton, T., Montelione, G., & Tong, L. Crystal Structure of AGR_C_4470p from Agrobacterium tumefaciens. United States. doi:10.1110/ps.062663307.
Vorobiev,S., Neely, H., Seetharaman, J., Ma, L., Xiao, R., Acton, T., Montelione, G., and Tong, L. Mon . "Crystal Structure of AGR_C_4470p from Agrobacterium tumefaciens". United States. doi:10.1110/ps.062663307.
@article{osti_930404,
title = {Crystal Structure of AGR_C_4470p from Agrobacterium tumefaciens},
author = {Vorobiev,S. and Neely, H. and Seetharaman, J. and Ma, L. and Xiao, R. and Acton, T. and Montelione, G. and Tong, L.},
abstractNote = {We report here the crystal structure at 2.0 {angstrom} 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.},
doi = {10.1110/ps.062663307},
journal = {Protein Science},
number = ,
volume = 16,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}