User:Eduardo Soares/Sandbox 1
From Proteopedia
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==Introduction== | ==Introduction== | ||
The PDB code 2RDE represents a PilZ protein complexed with cyclic diguanylate monophosphate (c-di-GMP) there is a molecular interaction involved in the regulation of bacterial biofilm formation and motility. The complex is formed by the binding of the small signaling molecule c-di-GMP to a protein domain known as PilZ. This interaction plays a crucial role in bacterial physiology and is implicated in various cellular processes. | The PDB code 2RDE represents a PilZ protein complexed with cyclic diguanylate monophosphate (c-di-GMP) there is a molecular interaction involved in the regulation of bacterial biofilm formation and motility. The complex is formed by the binding of the small signaling molecule c-di-GMP to a protein domain known as PilZ. This interaction plays a crucial role in bacterial physiology and is implicated in various cellular processes. | ||
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| + | == PilZ domain== | ||
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| + | The concept of PilZ Domains as c-di-GMP Effectors is supported by compelling bioinformatics analysis. PilZ domains, typically located at the C-terminus of cellulose synthetase, produced by the bcsA gene, have been proposed to act as effectors for the signaling molecule cyclic diguanylate monophosphate (c-di-GMP). The discovery that c-di-GMP functions as an allosteric regulator of cellulose synthetase in Gluconacetobacter xylinus, as demonstrated by Benziman and colleagues, represented a significant breakthrough in the field. | ||
| + | Notably, the PilZ protein in Pseudomonas aeruginosa contains a single 118-residue domain exhibiting substantial sequence similarity to the C-terminus of BcsA. Within the pil operon, responsible for the synthesis and functionality of pili, PilZ is among the few proteins with an unknown function. This operon plays a role in the transition from motile to sessile growth modes, although the precise regulatory mechanisms remain elusive. Strains lacking the PilZ domain (ΔpilZ) can produce normal levels of pilin protomers but are unable to assemble functional pili. | ||
| + | Furthermore, other PilZ-domain proteins have been implicated in the regulation of motility across various organisms. For instance, the YcgR protein in Escherichia coli and the DgrA and DgrB proteins in Caulobacter crescentus have demonstrated involvement in controlling motility under high cytosolic c-di-GMP concentrations. Notably, certain PilZ domains are situated at the C-terminus of proteins participating in processes sensitive to c-di-GMP levels. Alg44 from P. aeruginosa represents another example, functioning as an essential protein in the c-di-GMP-regulated process of alginate biosynthesis. These discoveries provide robust evidence supporting the hypothesis that the majority of PilZ domains function as effectors, binding c-di-GMP, and exerting a critical role in the regulation of various cellular processes. | ||
<StructureSection load='2rde' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='2rde' size='340' side='right' caption='Caption for this structure' scene=''> | ||
Revision as of 11:49, 23 June 2023
Contents |
VCA0042/plzD complexed with c-di-GMP
Introduction
The PDB code 2RDE represents a PilZ protein complexed with cyclic diguanylate monophosphate (c-di-GMP) there is a molecular interaction involved in the regulation of bacterial biofilm formation and motility. The complex is formed by the binding of the small signaling molecule c-di-GMP to a protein domain known as PilZ. This interaction plays a crucial role in bacterial physiology and is implicated in various cellular processes.
PilZ domain
The concept of PilZ Domains as c-di-GMP Effectors is supported by compelling bioinformatics analysis. PilZ domains, typically located at the C-terminus of cellulose synthetase, produced by the bcsA gene, have been proposed to act as effectors for the signaling molecule cyclic diguanylate monophosphate (c-di-GMP). The discovery that c-di-GMP functions as an allosteric regulator of cellulose synthetase in Gluconacetobacter xylinus, as demonstrated by Benziman and colleagues, represented a significant breakthrough in the field. Notably, the PilZ protein in Pseudomonas aeruginosa contains a single 118-residue domain exhibiting substantial sequence similarity to the C-terminus of BcsA. Within the pil operon, responsible for the synthesis and functionality of pili, PilZ is among the few proteins with an unknown function. This operon plays a role in the transition from motile to sessile growth modes, although the precise regulatory mechanisms remain elusive. Strains lacking the PilZ domain (ΔpilZ) can produce normal levels of pilin protomers but are unable to assemble functional pili. Furthermore, other PilZ-domain proteins have been implicated in the regulation of motility across various organisms. For instance, the YcgR protein in Escherichia coli and the DgrA and DgrB proteins in Caulobacter crescentus have demonstrated involvement in controlling motility under high cytosolic c-di-GMP concentrations. Notably, certain PilZ domains are situated at the C-terminus of proteins participating in processes sensitive to c-di-GMP levels. Alg44 from P. aeruginosa represents another example, functioning as an essential protein in the c-di-GMP-regulated process of alginate biosynthesis. These discoveries provide robust evidence supporting the hypothesis that the majority of PilZ domains function as effectors, binding c-di-GMP, and exerting a critical role in the regulation of various cellular processes.
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
