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TitleEngineering enzyme stability and resistance to an organic cosolvent by modification of residues in the access tunnel.
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 52, Page 1959-1963, Year 2013
Publish dateMay 14, 2012 (structure data deposition date)
AuthorsKoudelakova, T. / Chaloupkova, R. / Brezovsky, J. / Prokop, Z. / Sebestova, E. / Hesseler, M. / Khabiri, M. / Plevaka, M. / Kulik, D. / Kuta Smatanova, I. ...Koudelakova, T. / Chaloupkova, R. / Brezovsky, J. / Prokop, Z. / Sebestova, E. / Hesseler, M. / Khabiri, M. / Plevaka, M. / Kulik, D. / Kuta Smatanova, I. / Rezacova, P. / Ettrich, R. / Bornscheuer, U.T. / Damborsky, J.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:23303607
MethodsX-ray diffraction
Resolution1.2 - 1.45 Å
Structure data

PDB-4f5z:
Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (L95V, A172V).
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-4f60:
Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-BEZ:
BENZOIC ACID

ChemComp-HOH:
WATER

ChemComp-F:
FLUORIDE ION

Source
  • rhodococcus rhodochrous (bacteria)
KeywordsHYDROLASE / mutation in access tunnel

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