2Z8M

Structural basis for the catalytic mechanism of phosphothreonine lyase

Summary for 2Z8M

• Entry DOI: 10.2210/pdb2z8m/pdb
• Related: 2Z8N 2Z8O 2Z8P
• Descriptor: 27.5 kDa virulence protein (2 entities in total)
• Functional Keywords: short three-helix bundle, distorted beta-strand sheet, virulence, lyase
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 2
• Total formula weight: 55362.28

Authors

Chen, L.,Wang, H.,Gu, L.,Huang, N.,Zhou, J.M.,Chai, J. (deposition date: 2007-09-07, release date: 2007-12-18, Last modification date: 2023-11-01)

Primary citation

Chen, L.,Wang, H.,Zhang, J.,Gu, L.,Huang, N.,Zhou, J.M.,Chai, J.
Structural basis for the catalytic mechanism of phosphothreonine lyase.
Nat.Struct.Mol.Biol., 15:101-102, 2008

PubMed Abstract: Salmonella SpvC belongs to a new enzyme family designated phosphothreonine lyases that irreversibly inactivate mitogen-activated protein kinases. The crystal structure of SpvC reported here reveals that the two phosphorylated residues in the substrate peptide predominantly mediate its recognition by SpvC. Substrate-induced conformational changes in SpvC sequester the phosphothreonine in a completely solvent-free environment, preventing the hydrolysis of the phosphate group and facilitating the elimination reaction.

PubMed: 18084305
DOI: 10.1038/nsmb1329

Experimental method

X-RAY DIFFRACTION (2 Å)