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TitleStructural and mechanistic exploration of Acid resistance: kinetic stability facilitates evolution of extremophilic behavior
Journal, issue, pagesJ. Mol. Biol., Vol. 368, Page 870-883, Year 2007
Publish dateFeb 9, 2007 (structure data deposition date)
AuthorsKelch, B.A. / Eagen, K.P. / Erciyas, F.P. / Humphris, E.L. / Thomason, A.R. / Mitsuiki, S. / Agard, D.A.
External linksJ. Mol. Biol. / PubMed:17382344
MethodsX-ray diffraction
Resolution1.85 Å
Structure data

PDB-2oua:
Crystal Structure of Nocardiopsis Protease (NAPase)
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-AES:
4-(2-AMINOETHYL)BENZENESULFONYL FLUORIDE / protease inhibitor*YM

ChemComp-DIO:
1,4-DIETHYLENE DIOXIDE

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • nocardiopsis alba (bacteria)
Keywordshydrolase/hydrolase inhibitor / serine protease; kinetic stability; acid stability; electrostatics / HYDROLASE / hydrolase-hydrolase inhibitor complex

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