Rhomboid protease

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   Print3D 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. 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). Whole active site. Water molecules shown as red spheres.

3D Structures of rhomboid protease

Updated on 10-August-2016

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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
    
  • 4qnz – EcGlpG core region (mutant) + peptide inhibitor
    
  • 4qo0, 4qo2, 5f5g, 5f5b – EcGlpG core region + peptide inhibitor
    

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Michal Harel, Alexander Berchansky, Joel L. Sussman