2H5Y

Crystallographic structure of the Molybdate-Binding Protein of Xanthomonas citri at 1.7 Ang resolution bound to molybdate

Summary for 2H5Y

• Entry DOI: 10.2210/pdb2h5y/pdb
• Related: 1AMF 1ATZ
• Descriptor: Molybdate-binding periplasmic protein, SULFATE ION, MOLYBDATE ION, ... (4 entities in total)
• Functional Keywords: molybdate-binding protein, moda, xanthomonas axonopodis pv. citri, metal transport
• Biological source: Xanthomonas axonopodis pv. citri
• Total number of polymer chains: 3
• Total formula weight: 80952.63

Authors

Balan, A.,Santacruz, C.P.,Ferreira, L.C.S.,Barbosa, J.A.R.G. (deposition date: 2006-05-29, release date: 2007-06-05, Last modification date: 2023-10-25)

Primary citation

Santacruz, C.P.,Balan, A.,Ferreira, L.C.,Barbosa, J.A.R.G.
Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri
Acta Crystallogr.,Sect.F, 62:289-291, 2006

PubMed Abstract: Xanthomonas axonopodis pv. citri ModA protein is the ABC periplasmic binding component responsible for the capture of molybdate. The protein was crystallized with sodium molybdate using the hanging-drop vapour-diffusion method in the presence of PEG or sulfate. X-ray diffraction data were collected to a maximum resolution of 1.7 A using synchrotron radiation. The crystal belongs to the orthorhombic space group C222(1), with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 A. The crystal structure was solved by molecular-replacement methods and structure refinement is in progress.

PubMed: 16511325
DOI: 10.1107/S1744309106003812

Experimental method

X-RAY DIFFRACTION (1.7 Å)