5XLY

Crystal structure of CheR1 in complex with c-di-GMP-bound MapZ

Summary for 5XLY

• Entry DOI: 10.2210/pdb5xly/pdb
• Descriptor: Chemotaxis protein methyltransferase 1, Cyclic diguanosine monophosphate-binding protein PA4608, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), ... (4 entities in total)
• Functional Keywords: signaling, methyltransferase, transferase
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1); More
• Total number of polymer chains: 2
• Total formula weight: 48662.80

Authors

Yuan, Z.,Zhu, Y.,Gu, L. (deposition date: 2017-05-12, release date: 2017-08-23, Last modification date: 2024-03-27)

Primary citation

Zhu, Y.,Yuan, Z.,Gu, L.
Structural basis for the regulation of chemotaxis by MapZ in the presence of c-di-GMP
Acta Crystallogr D Struct Biol, 73:683-691, 2017

PubMed Abstract: The bacterial second messenger cyclic diguanylate monophosphate (c-di-GMP) mediates multiple aspects of bacterial physiology through binding to various effectors. In some cases, these effectors are single-domain proteins which only contain a PilZ domain. It remains largely unknown how single-domain PilZ proteins function and regulate their downstream targets. Recently, a single-domain PilZ protein, MapZ (PA4608), was identified to inhibit the activity of the methyltransferase CheR1. Here, crystal structures of the C-terminal domain of CheR1 containing SAH and of CheR1 in complex with c-di-GMP-bound MapZ are reported. It was observed that the binding site of MapZ in CheR1 partially overlaps with the SAH/SAM-binding pocket. Consequently, binding of MapZ blocks SAH/SAM binding. This provides direct structural evidence on the mechanism of inhibition of CheR1 by MapZ in the presence of c-di-GMP.

PubMed: 28777083
DOI: 10.1107/S2059798317009998

Experimental method

X-RAY DIFFRACTION (1.763 Å)