5XLX

Crystal structure of the C-terminal domain of CheR1 containing SAH

Summary for 5XLX

• Entry DOI: 10.2210/pdb5xlx/pdb
• Descriptor: Chemotaxis protein methyltransferase 1, S-ADENOSYL-L-HOMOCYSTEINE (3 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)
• Total number of polymer chains: 4
• Total formula weight: 128560.03

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 (1.969 Å)