Structural highlights
Function
[CHER1_PSEAE] Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. [CDGBP_PSEAE] Binds the second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP). Can bind two c-di-GMP molecules per monomer. May play a role in bacterial second-messenger regulated processes. Binding to c-di-GMP induces a conformational change of the C- and N-termini resulting in the exposure of a highly negative surface on one side of the protein to a possible effector protein.[1] [2] [3]
Publication Abstract from PubMed
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.
Structural basis for the regulation of chemotaxis by MapZ in the presence of c-di-GMP.,Zhu Y, Yuan Z, Gu L Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):683-691. doi:, 10.1107/S2059798317009998. Epub 2017 Jul 28. PMID:28777083[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ramelot TA, Yee A, Cort JR, Semesi A, Arrowsmith CH, Kennedy MA. NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Proteins. 2007 Feb 1;66(2):266-71. PMID:17096419 doi:10.1002/prot.21199
- ↑ Shin JS, Ryu KS, Ko J, Lee A, Choi BS. Structural characterization reveals that a PilZ domain protein undergoes substantial conformational change upon binding to cyclic dimeric guanosine monophosphate. Protein Sci. 2011 Feb;20(2):270-7. doi: 10.1002/pro.557. Epub 2010 Dec 23. PMID:21280119 doi:http://dx.doi.org/10.1002/pro.557
- ↑ Habazettl J, Allan MG, Jenal U, Grzesiek S. Solution structure of the PilZ domain protein PA4608 complex with c-di-GMP identifies charge clustering as molecular readout. J Biol Chem. 2011 Feb 10. PMID:21310957 doi:10.1074/jbc.M110.209007
- ↑ 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. 2017 Aug 1;73(Pt 8):683-691. doi:, 10.1107/S2059798317009998. Epub 2017 Jul 28. PMID:28777083 doi:http://dx.doi.org/10.1107/S2059798317009998
