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- PDB-1aiw: NMR STRUCTURES OF THE CELLULOSE-BINDING DOMAIN OF THE ENDOGLUCANA... -

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Entry
Database: PDB / ID: 1aiw
TitleNMR STRUCTURES OF THE CELLULOSE-BINDING DOMAIN OF THE ENDOGLUCANASE Z FROM ERWINIA CHRYSANTHEMI, 23 STRUCTURES
ComponentsENDOGLUCANASE Z
KeywordsCELLULOSE DEGRADATION / ENDOGLUCANASE / CELLULOSE-BINDING DOMAIN / ERWINIA CHRYSANTHEMI
Function / homology
Function and homology information


cellulase / cellulase activity / cellulose catabolic process / carbohydrate binding / extracellular region
Similarity search - Function
Endoglucanase Z, cellulose-binding domain / Cellulose-binding domain / Carbohydrate-binding module superfamily 5/12 / Seminal Fluid Protein PDC-109 (Domain B) / Chitin-binding domain type 3 / Carbohydrate-binding module family 5/12 / Carbohydrate-binding module superfamily 5/12 / Glycoside hydrolase, family 5, conserved site / Glycosyl hydrolases family 5 signature. / Glycoside hydrolase, family 5 ...Endoglucanase Z, cellulose-binding domain / Cellulose-binding domain / Carbohydrate-binding module superfamily 5/12 / Seminal Fluid Protein PDC-109 (Domain B) / Chitin-binding domain type 3 / Carbohydrate-binding module family 5/12 / Carbohydrate-binding module superfamily 5/12 / Glycoside hydrolase, family 5, conserved site / Glycosyl hydrolases family 5 signature. / Glycoside hydrolase, family 5 / Cellulase (glycosyl hydrolase family 5) / Ribbon / Glycoside hydrolase superfamily / Mainly Beta
Similarity search - Domain/homology
Biological speciesErwinia chrysanthemi (bacteria)
MethodSOLUTION NMR / SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS
AuthorsBrun, E. / Moriaud, F. / Gans, P. / Blackledge, M.J. / Barras, F. / Marion, D.
Citation
Journal: Biochemistry / Year: 1997
Title: Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi.
Authors: Brun, E. / Moriaud, F. / Gans, P. / Blackledge, M.J. / Barras, F. / Marion, D.
#1: Journal: Eur.J.Biochem. / Year: 1995
Title: Overproduction, Purification and Characterization of the Cellulose-Binding Domain of the Erwinia Chrysanthemi Secreted Endoglucanase Egz
Authors: Brun, E. / Gans, P. / Marion, D. / Barras, F.
#2: Journal: Mol.Microbiol. / Year: 1994
Title: Periplasmic Disulphide Bond Formation is Essential for Cellulase Secretion by the Plant Pathogen Erwinia Chrysanthemi
Authors: Bortoli-German, I. / Brun, E. / Py, B. / Chippaux, M. / Barras, F.
#3: Journal: Protein Eng. / Year: 1991
Title: Cellulase Egz of Erwinia Chrysanthemi: Structural Organization and Importance of His98 and Glu133 Residues for Catalysis
Authors: Py, B. / Bortoli-German, I. / Haiech, J. / Chippaux, M. / Barras, F.
History
DepositionApr 30, 1997Processing site: BNL
Revision 1.0May 6, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.3Jun 5, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_nmr_software
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name
Revision 1.4Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ENDOGLUCANASE Z


Theoretical massNumber of molelcules
Total (without water)6,6601
Polymers6,6601
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)23 / 30LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein ENDOGLUCANASE Z / CBDEGZ


Mass: 6660.123 Da / Num. of mol.: 1 / Fragment: C-TERMINAL CELLULOSE-BINDING DOMAIN / Mutation: T1M, A2G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Erwinia chrysanthemi (bacteria) / Genus: Dickeya / Strain: 3937 / Cell line: BL21 / Cellular location: SECRETED / Gene: CELZ / Plasmid: PET22 / Species (production host): Escherichia coli / Cellular location (production host): EXTRACELLULAR / Gene (production host): PMIA2 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P07103, cellulase
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111DQF-COSY
121TOCSY
131NOESY

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Sample preparation

Sample conditionspH: 4.6 / Temperature: 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX 600 / Manufacturer: Bruker / Model: AMX 600 / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DiscoverBIOSYMrefinement
BIOSYM DISCOVERDISCOVERstructure solution
RefinementMethod: SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 30 / Conformers submitted total number: 23

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