3W9S

Crystal Structure Analysis of the N-terminal Receiver domain of Response Regulator PmrA

Summary for 3W9S

• Entry DOI: 10.2210/pdb3w9s/pdb
• Descriptor: OmpR family response regulator in two-component regulatory system with BasS, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: alpha and beta proteins, rossmann fold topology, polymyxin b resistant protein a, response regulator, signaling protein-antimicrobial protein complex, signaling protein/antimicrobial protein
• Biological source: Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044
• Total number of polymer chains: 2
• Total formula weight: 29696.28

Authors

Chen, C.,Luo, S. (deposition date: 2013-04-15, release date: 2013-07-24, Last modification date: 2023-11-08)

Primary citation

Lou, S.C.,Lou, Y.C.,Rajasekaran, M.,Chang, Y.W.,Hsiao, C.D.,Chen, C.
Structural Basis of a Physical Blockage Mechanism for the Interaction of Response Regulator PmrA with Connector Protein PmrD from Klebsiella Pneumoniae
J.Biol.Chem., 288:25551-25561, 2013

PubMed Abstract: In bacteria, the two-component system is the most prevalent for sensing and transducing environmental signals into the cell. The PmrA-PmrB two-component system, responsible for sensing external stimuli of high Fe(3+) and mild acidic conditions, can control the genes involved in lipopolysaccharide modification and polymyxin resistance in pathogens. In Klebsiella pneumoniae, the small basic connector protein PmrD protects phospho-PmrA and prolongs the expression of PmrA-activated genes. We previously determined the phospho-PmrA recognition mode of PmrD. However, how PmrA interacts with PmrD and prevents its dephosphorylation remains unknown. To address this question, we solved the x-ray crystal structure of the N-terminal receiver domain of BeF3(-)-activated PmrA (PmrA(N)) at 1.70 Å. With this structure, we applied the data-driven docking method based on NMR chemical shift perturbation to generate the complex model of PmrD-PmrA(N), which was further validated by site-directed spin labeling experiments. In the complex model, PmrD may act as a blockade to prevent phosphatase from contacting with the phosphorylation site on PmrA.

PubMed: 23861396
DOI: 10.1074/jbc.M113.481978

Experimental method

X-RAY DIFFRACTION (1.7 Å)