5Y4R

Structure of a methyltransferase complex

Summary for 5Y4R

• Entry DOI: 10.2210/pdb5y4r/pdb
• Descriptor: Chemotaxis protein methyltransferase 1, Cyclic diguanosine monophosphate-binding protein PA4608, SULFATE ION, ... (5 entities in total)
• Functional Keywords: complex, transferase-protein binding complex, transferase/protein binding
• Biological source: Pseudomonas aeruginosa str. PAO1; More
• Total number of polymer chains: 4
• Total formula weight: 103827.65

Authors

Yan, X.,Xin, L.,Tan, Y.J.,Jin, S.,Liang, Z.X.,Gao, Y.G. (deposition date: 2017-08-04, release date: 2017-11-29, Last modification date: 2023-11-22)

Primary citation

Yan, X.F.,Xin, L.,Yen, J.T.,Zeng, Y.,Jin, S.,Cheang, Q.W.,Fong, R.A.C.Y.,Chiam, K.H.,Liang, Z.X.,Gao, Y.G.
Structural analyses unravel the molecular mechanism of cyclic di-GMP regulation of bacterial chemotaxis via a PilZ adaptor protein.
J. Biol. Chem., 293:100-111, 2018

PubMed Abstract: The bacterial second messenger cyclic di-GMP (c-di-GMP) has emerged as a prominent mediator of bacterial physiology, motility, and pathogenicity. c-di-GMP often regulates the function of its protein targets through a unique mechanism that involves a discrete PilZ adaptor protein. However, the molecular mechanism for PilZ protein-mediated protein regulation is unclear. Here, we present the structure of the PilZ adaptor protein MapZ cocrystallized in complex with c-di-GMP and its protein target CheR1, a chemotaxis-regulating methyltransferase in This cocrystal structure, together with the structure of free CheR1, revealed that the binding of c-di-GMP induces dramatic structural changes in MapZ that are crucial for CheR1 binding. Importantly, we found that restructuring and repositioning of two C-terminal helices enable MapZ to disrupt the CheR1 active site by dislodging a structural domain. The crystallographic observations are reinforced by protein-protein binding and single cell-based flagellar motor switching analyses. Our studies further suggest that the regulation of chemotaxis by c-di-GMP through MapZ orthologs/homologs is widespread in proteobacteria and that the use of allosterically regulated C-terminal motifs could be a common mechanism for PilZ adaptor proteins. Together, the findings provide detailed structural insights into how c-di-GMP controls the activity of an enzyme target indirectly through a PilZ adaptor protein.

PubMed: 29146598
DOI: 10.1074/jbc.M117.815704

Experimental method

X-RAY DIFFRACTION (2.298 Å)