2BZB

NMR Solution Structure of a protein aspartic acid phosphate phosphatase from Bacillus Anthracis

Summary for 2BZB

• Entry DOI: 10.2210/pdb2bzb/pdb
• NMR Information: BMRB: 7350
• Descriptor: CONSERVED DOMAIN PROTEIN (1 entity in total)
• Functional Keywords: transferase, phosphatase, phosphorylation, sporulation, bacillus, anthracis, antithetical, negative, regulator, spine
• Biological source: BACILLUS ANTHRACIS
• Total number of polymer chains: 2
• Total formula weight: 15031.75

Authors

Grenha, R.,Rzechorzek, N.J.,Brannigan, J.A.,Ab, E.,Folkers, G.E.,De Jong, R.N.,Diercks, T.,Wilkinson, A.J.,Kaptein, R.,Wilson, K.S. (deposition date: 2005-08-14, release date: 2006-09-25, Last modification date: 2018-05-09)

• Primary citation: Grenha, R.,Rzechorzek, N.J.,Brannigan, J.A.,de Jong, R.N.,Ab, E.,Diercks, T.,Truffault, V.,Ladds, J.C.,Fogg, M.J.,Bongiorni, C.,Perego, M.,Kaptein, R.,Wilson, K.S.,Folkers, G.E.,Wilkinson, A.J.; Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli.; J. Biol. Chem., 281:37993-38003, 2006; PubMed: 17001075; DOI: 10.1074/jbc.M607617200

Experimental method

SOLUTION NMR