3SFT: Crystal Structure Of Thermotoga Maritima Cheb Methylesterase Catalytic Domain

We have determined 2.2 A resolution crystal structure of Thermotoga maritima CheB methylesterase domain to provide insight into the interaction mode between CheB and chemoreceptors. T. maritima CheB methylesterase domain has identical topology of a modified doubly-wound alpha/beta fold that was observed from the previously reported Salmonella typhimurium counterpart, but the analysis of the electrostatic potential surface near the catalytic triad indicated considerable charge distribution difference. As the CheB demethylation consensus sites of the chemoreceptors, the CheB substrate, are not uniquely conserved between T. maritima and S. typhimurium, such surfaces with differing electrostatic properties may reflect CheB regions that mediate protein-protein interaction. Via the computational docking of the two T. maritima and S. typhimurium CheB structures to the respective T. maritima and Escherichia coli chemoreceptors, we propose a CheB:chemoreceptor interaction mode.
PDB ID: 3SFTDownload
MMDB ID: 92213
PDB Deposition Date: 2011/6/14
Updated in MMDB: 2011/07
Experimental Method:
x-ray diffraction
Resolution: 2.15  Å
Source Organism:
Similar Structures:
Biological Unit for 3SFT: monomeric; determined by author and by software (PISA)
Molecular Components in 3SFT
Label Count Molecule
Protein (1 molecule)
Chemotaxis Response Regulator Protein-glutamate Methylesterase(Gene symbol: TM0408)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB