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Anisotropic refinement of the structure of Thermoascus aurantiacusxylanase I

Teixeira, S., Lo Leggio, L., Pickersgill, R. and Cardin, C. (2001) Anisotropic refinement of the structure of Thermoascus aurantiacusxylanase I. Acta Crystallographica Section D - Biological Crystallography, 57 (3). pp. 385-392. ISSN 1399-0047

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To link to this article DOI: 10.1107/S0907444900019089

Abstract/Summary

The isotropic crystallographic model of the structure of xylanase I from Thermoascus aurantiacus (TAXI) has now been refined anisotropically at 1.14 Å resolution to a standard residual of R = 11.1% for all data. TAXI is amongst the five largest proteins deposited in the Protein Data Bank to have been refined with anisotropic displacement parameters (ADPs) at this level of resolution. The anisotropy analysis revealed a more isotropic distribution of anisotropy than usually observed previously. Adding ADPs resulted in high-quality electron-density maps which revealed discrepancies from the previously suggested primary sequences for this enzyme. Side-chain conformational disorder was modelled for 16 residues, including Trp275, a bulky residue at the active site. An unrestrained refinement was consistent with the protonation of the catalytic acid/base glutamate and the deprotonation of the nucleophile glutamate, as required for catalysis. The thermal stability of TAXI is reinterpreted in the light of the new refined model.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:23745
Uncontrolled Keywords:xylanases
Publisher:Wiley

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