Substrate specificity and subsite mobility in T. aurantiacus xylanase 10A
- 27 November 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 509 (2) , 303-308
- https://doi.org/10.1016/s0014-5793(01)03177-5
Abstract
The substrate specificity of Thermoascus aurantiacus xylanase 10A (TAX) has been investigated both biochemically and structurally. High resolution crystallographic analyses at 291 K and 100 K of TAX complexes with xylobiose show that the ligand is in its α anomeric conformation and provide a rationale for specificity on p‐nitrophenyl glycosides at the −1 and −2 subsites. Trp 275, which is disordered in uncomplexed structures, is stabilised by its interaction with xylobiose. Two structural subsets in family 10 are identified, which differ by the presence or absence of a short helical stretch in the eighth βα‐loop of the TIM barrel, the loop bearing Trp 275. This structural difference is discussed in the context of Trp 275 mobility and xylanase function.Keywords
This publication has 35 references indexed in Scilit:
- Plant Enzyme Structure. Explaining Substrate Specificity and the Evolution of FunctionPlant Physiology, 2001
- Crystal structure of Streptomyces olivaceoviridis E-86 β-xylanase containing xylan-binding domainJournal of Molecular Biology, 2000
- Crystal structure at 1.8 Å resolution and proposed amino acid sequence of a thermostable xylanase from Thermoascus aurantiacusJournal of Molecular Biology, 1999
- Structure of the xylanase from Penicillium simplicissimumProtein Science, 1998
- Insights into transition state stabilization of the β-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutantsNature Structural & Molecular Biology, 1998
- Exploring the Cellulose/Xylan Specificity of the β-1,4-Glycanase Cex from Cellulomonas fimi through Crystallography and Mutation,Biochemistry, 1998
- Structure of the Bacillus agaradherans Family 5 Endoglucanase at 1.6 Å and Its Cellobiose Complex at 2.0 Å Resolution,Biochemistry, 1998
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- β‐Glucosidase, β‐galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes wit 8‐fold β/α architecture and with two conserved glutamates near the carboxy‐terminal ends of β‐strands four and sevenFEBS Letters, 1995
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991