Rhomboid protease

From Proteopedia

spinqualitylabelsall models Structure of rhomboid protease complex with inhibitor isocoumarin and nonyglucoside detergent molecules (PDB entry 2xow) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Rhomboid protease (GlpG) is a transmembranal serine protease. The active site is buried in the lipid bilayer of cell membrane. It cleaves proteins within their transmembrane domain[1]. Rhomboids regulate many cellular processes and are involved in many human diseases. The catalytic site of rhomboids contains a hydrophilic pocket protected from the lipid bilayer. Rhomboids are specific for a single transmembranal helix proteins. Rhomboid protease YqgP interacts with the membrane bound metlloprotease FisH and cleaves the high-affinity Mg transporter[2]. Structural highlights The inhibitor (in deepskyblue)[3]. . Water molecules shown as red spheres.

3D Structures of rhomboid protease

Updated on 08-August-2024

References

1. ↑ Freeman M. Rhomboid proteases and their biological functions. Annu Rev Genet. 2008;42:191-210. doi: 10.1146/annurev.genet.42.110807.091628. PMID:18605900 doi:http://dx.doi.org/10.1146/annurev.genet.42.110807.091628
2. ↑ Began J, Cordier B, Brezinova J, Delisle J, Hexnerova R, Srb P, Rampirova P, Kozisek M, Baudet M, Coute Y, Galinier A, Veverka V, Doan T, Strisovsky K. Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease. EMBO J. 2020 Jan 13:e102935. doi: 10.15252/embj.2019102935. PMID:31930742 doi:http://dx.doi.org/10.15252/embj.2019102935
3. ↑ Vinothkumar KR, Strisovsky K, Andreeva A, Christova Y, Verhelst S, Freeman M. The structural basis for catalysis and substrate specificity of a rhomboid protease. EMBO J. 2010 Oct 1. PMID:20890268 doi:10.1038/emboj.2010.243