| 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.
Structural highlights
The inhibitor isocoumarin covalently binds to the GlpG catalytic residues Ser and His (in deepskyblue)[2]. Whole active site. Water molecules shown as red spheres.
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3D Structures of rhomboid protease
Updated on 27-August-2019
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- Rhomboid protease
- 2ic8, 2irv, 2nrf, 2o7l, 3b45, 2xov, 4njn, 4njp – EcGlpG core region – Escherichia coli
- 2xtu, 3b44, 2xtv, 5f5d – EcGlpG core region (mutant)
- 4hdd – EcGlpG N terminal
- 2lep, 2mja – EcGlpG N terminal - NMR
- 3odj – HiGlpG - Haemophilus influenzae
- 2nr9 – HiGlpG (mutant) + detergent
- 2gqc – RP N terminal – NMR – Pseudomonas aeruginosa
- Rhomboid protease complex with inhibitor
- 2xow, 3zeb – EcGlpG core region + isocoumarin inhibitor
- 3txt, 4h1d – EcGlpG core region + DFP inhibitor
- 3ubb – EcGlpG core region + phosphonofluoridate inhibitor
- 3zmh, 3zmi, 3zmj, 3zot – EcGlpG core region + β-lactam inhibitor
- 5f5j, 5f5k – EcGlpG core region (mutant) + aldehyde inhibitor
- 4qo0, 4qo2, 5f5g, 5f5b, 5mtf, 5mt6, 5mt7, 5mt8 – EcGlpG core region + peptide inhibitor
- 4qnz – EcGlpG core region (mutant) + peptide inhibitor
References
