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-Structure paper
Title | Structural basis for the selectivity of the external thioesterase of the surfactin synthetase. |
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Journal, issue, pages | Nature, Vol. 454, Page 907-911, Year 2008 |
Publish date | Apr 10, 2008 (structure data deposition date) |
Authors | Koglin, A. / Lohr, F. / Bernhard, F. / Rogov, V.V. / Frueh, D.P. / Strieter, E.R. / Mofid, M.R. / Guntert, P. / Wagner, G. / Walsh, C.T. ...Koglin, A. / Lohr, F. / Bernhard, F. / Rogov, V.V. / Frueh, D.P. / Strieter, E.R. / Mofid, M.R. / Guntert, P. / Wagner, G. / Walsh, C.T. / Marahiel, M.A. / Dotsch, V. |
External links | Nature / PubMed:18704089 |
Methods | NMR (solution) |
Structure data | PDB-2k2q: PDB-2ron: |
Source |
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Keywords | Ligase/Hydrolase / thioesterase / a/b-hydrolase / NRPS / non-ribosomal peptide synthetase / type II thioesterase / Antibiotic biosynthesis / Ligase / Multifunctional enzyme / Phosphopantetheine / Sporulation / Stress response / Ligase-Hydrolase COMPLEX / HYDROLASE / TEII / a/b hydrolase / PCP regeneration |