2HQV

X-ray Crystal Structure of Protein AGR_C_4470 from Agrobacterium tumefaciens. Northeast Structural Genomics Consortium Target AtR92.

Summary for 2HQV

• Entry DOI: 10.2210/pdb2hqv/pdb
• Descriptor: AGR_C_4470p (2 entities in total)
• Functional Keywords: nesg, atr92, agr_c_4470, q7cx01_agrt5, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, unknown function
• Biological source: Agrobacterium tumefaciens str. C58
• Total number of polymer chains: 1
• Total formula weight: 21620.75

Authors

Vorobiev, S.M.,Neely, H.,Seetharaman, J.,Zhao, L.,Cunningham, K.,Ma, L.C.,Fang, Y.,Xiao, R.,Acton, T.,Montelione, T.G.,Hunt, J.F.,Tong, L.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2006-07-19, release date: 2006-09-19, Last modification date: 2024-10-30)

Primary citation

Vorobiev, S.M.,Neely, H.,Seetharaman, J.,Ma, L.C.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Tong, L.
Crystal structure of AGR_C_4470p from Agrobacterium tumefaciens.
Protein Sci., 16:535-538, 2007

PubMed Abstract: 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.

PubMed: 17322535
DOI: 10.1110/ps.062663307

Experimental method

X-RAY DIFFRACTION (2 Å)