Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens (Q27641622)

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Gideon Davies

object named as

Gideon J Davies

8

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author name string

Torben P Frandsen

2

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Ingemar von Ossowski

3

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Viviane Boyer

4

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Hugues Driguez

6

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Martin Schülein

Fine substrate specificities of four exo-type cellulases produced by Aspergillus niger, Trichoderma reesei, and Irpex lacteus on (1-->3), (1-->4)-beta-D-glucans and xyloglucan

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publication date

July 2003

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published in

Structure

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volume

11

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issue

7

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page(s)

855-64

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cites work

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Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose

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Site-directed mutation of the putative catalytic residues of endoglucanase CenA from Cellulomonas fimi

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Structures and mechanisms of glycosyl hydrolases

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Crystal structure of beta-D-cellotetraose hemihydrate with implications for the structure of cellulose II.

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A simple and rapid method for generating a deletion by PCR

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Phi/psi-chology: Ramachandran revisited

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Tryptophan 272: an essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A.

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The active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175

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STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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The binding specificity and affinity determinants of family 1 and family 3 cellulose binding modules

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Ethanol production from biomass: technology and commercialization status

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Enhanced production of Trichoderma reesei endoglucanases and use of the new cellulase preparations in producing the stonewashed effect on denim fabric

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Processing of X-ray diffraction data collected in oscillation mode

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Crystal structures of the cellulase Cel48F in complex with inhibitors and substrates give insights into its processive action

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Improved Fourier coefficients for maps using phases from partial structures with errors

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Crystallization of the catalytic domain of Clostridium cellulolyticum CeLF cellulase in the presence of a newly synthesized cellulase inhibitor

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Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei

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Catalytic mechanism of enzymic glycosyl transfer

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Trichoderma reesei has no true exo-cellulase: all intact and truncated cellulases produce new reducing end groups on cellulose

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Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 Å resolution

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Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding

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Structure of theHumicola insolenscellobiohydrolase Cel6A D416A mutant in complex with a non-hydrolysable substrate analogue, methyl cellobiosyl-4-thio-β-cellobioside, at 1.9 Å

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Distortion of a cellobio-derived isofagomine highlights the potential conformational itinerary of inverting β-glucosidasesElectronic supplementary information (ESI) available: details of data and structure quality for complex of cel6A with 1. See ht

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Use of TLS parameters to model anisotropic displacements in macromolecular refinement

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Clostridium thermocellum Xyn10B carbohydrate-binding module 22-2: the role of conserved amino acids in ligand binding

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Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reesei

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

release_h2tektzb6nff7cdumyj5xuiqay

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/h2tektzb6nff7cdumyj5xuiqay

24 November 2022

mapped directly with Wikidata item

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12842048

1 reference

Consolidated OpenCitations Corpus – April 2017