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4BMF

Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello- oligosaccharides

Summary for 4BMF
Entry DOI10.2210/pdb4bmf/pdb
NMR InformationBMRB: 4148
DescriptorENDOGLUCANASE EG-1 (1 entity in total)
Functional Keywordshydrolase, cellobiohydrolase
Biological sourceHYPOCREA JECORINA
Cellular locationSecreted: P07981
Total number of polymer chains1
Total formula weight4095.45
Authors
Mattinen, M.L.,Linder, M.,Drakenberg, T.,Annila, A. (deposition date: 2013-05-08, release date: 2013-05-22, Last modification date: 2024-11-20)
Primary citationMattinen, M.L.,Linder, M.,Drakenberg, T.,Annila, A.
Solution Structure of the Cellulose-Binding Domain of Endoglucanase I from Trichoderma Reesei and its Interaction with Cello-Oligosaccharides.
Eur.J.Biochem., 256:279-, 1998
Cited by
PubMed Abstract: The solution structure of a synthetic 38-residue cellulose-binding domain (CBD) of endoglucanase I from Trichoderma reesei (CBD(EGI)) was determined by two-dimensional 1H-NMR spectroscopy. 100 structures were generated from a total of 599 NOE derived distance restraints and 28 phi and 14 chi dihedral angle restraints. For the final set of 19 selected structures, the rms deviation about the mean structure was 0.83+/-0.26 A for all atoms and 0.50+/-0.22 A for the backbone atoms. The structure of CBD(EGI) was very similar to that of CBD of cellobiohydrolase I from T reesei (CBD(CBHI)). The backbone trace of CBD(EGI) followed closely the irregular triple-stranded antiparallel beta-sheet structure of CBD(CBHI). Moreover, apart from the different side chains of Trp7 (CBD(EGI)) and Tyr5 (CBD(CBHI)), the cellulose-binding face of CBD(EGI) was similar to that of CBD(CBHI) within the precision of the structures. Finally, the interaction between CBD(EGI) and soluble sugars was investigated using cellopentaose and cellohexaose as substrates. Experiments showed that the interactions between CBD(EGI) and cellobiose units of sugars are specific, supporting the previously presented model for the CBD binding to crystalline cellulose.
PubMed: 9760165
DOI: 10.1046/J.1432-1327.1998.2560279.X
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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