Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

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Daglichtkas onder de loep genomen
Swinkels, P. ; Zwart, H.F. de - \ 2011
TuinbouwTV
Op het Wageningen UR terrein in Bleiswijk staat de Daglichtkas. Peter Swinkels en Feije de Zwart geven tekst en uitleg.
Crystal structure and biochemical properties of a novel thermostable esterase containing an immunoglobulin-like domain
Levisson, M. ; Sun, L. ; Hendriks, S.N.A. ; Swinkels, P. ; Akveld, T. ; Bultema, J.B. ; Barendregt, A. ; Heuvel, R.H.H. van den; Dijkstra, B.W. ; Oost, J. van der; Kengen, S.W.M. - \ 2009
Journal of Molecular Biology 385 (2009)3. - ISSN 0022-2836 - p. 949 - 962.
thermotoga-maritima - protein assemblies - mass-spectrometry - resolution - sequence - crystallography - aminopeptidase - classification - inhibition - refinement
Comparative analysis of the genome of the hyperthermophilic bacterium Thermotoga maritima revealed a hypothetical protein (EstA) with typical esterase features. The EstA protein was functionally produced in Escherichia coli and purified to homogeneity. It indeed displayed esterase activity with optima at or above 95 degrees C and at pH 8.5, with a preference for esters with short acyl chains (C2-C10). Its 2.6-A-resolution crystal structure revealed a classical alpha/beta hydrolase domain with a catalytic triad consisting of a serine, an aspartate, and a histidine. EstA is irreversibly inhibited by the organophosphate paraoxon. A 3.0-A-resolution structure confirmed that this inhibitor binds covalently to the catalytic serine residue of EstA. Remarkably, the structure also revealed the presence of an N-terminal immunoglobulin (Ig)-like domain, which is unprecedented among esterases. EstA forms a hexamer both in the crystal and in solution. Electron microscopy showed that the hexamer in solution is identical with the hexamer in the crystal, which is formed by two trimers, with the N-terminal domains facing each other. Mutational studies confirmed that residues Phe89, Phe112, Phe116, Phe246, and Trp377 affect enzyme activity. A truncated mutant of EstA, in which the Ig-like domain was removed, showed only 5% of wild-type activity, had lower thermostability, and failed to form hexamers. These data suggest that the Ig-like domain plays an important role in the enzyme multimerization and activity of EstA
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