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Structure paper

TitleCrystal Structures and Inhibition Kinetics Reveal a Two-Stage Catalytic Mechanism with Drug Design Implications for Rhomboid Proteolysis.
Journal, issue, pagesMol. Cell, Vol. 61, Page 329-340, Year 2016
Publish dateDec 4, 2015 (structure data deposition date)
AuthorsCho, S. / Dickey, S.W. / Urban, S.
External linksMol. Cell / PubMed:26805573
MethodsX-ray diffraction
Resolution2.3 - 2.5 Å
Structure data

PDB-5f5b:
Structure of E.Coli GlpG complexed with peptidic inhibitor Ac-VRMA-CHO
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5f5d:
Crystal structures and Inhibition kinetics reveal a two-state catalytic mechanism with drug design implications for rhomboid proteolysis
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5f5g:
Structure of E.Coli GlpG Y205F mutant complexed with peptidic inhibitor Ac-RMA-CHO in the DMPC/CHAPSO bicelle
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5f5j:
E.coli GlpG Y205F mutant complexed with aldehyde inhibitor in DMPC/CHAPSO bicelle
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-5f5k:
E.Coli GlpG Y205F mutant complexed with aldehyde inhibitor in DMPC/CHAPSO bicelle
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • drosophila melanogaster (fruit fly)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Rhomboid / membrane protease / aldehyde inhibitor / HYDROLASE-INHIBITOR complex / HYDROLASE-HYDROLASE INHIBITOR complex / HYDROLASE / Intramembrane protease / Bicelle / GlpG

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