6D25

Crystal structure of the GH51 arabinofuranosidase from Xanthomonas axonopodis pv. citri


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.91 Å
  • R-Value Free: 0.167 
  • R-Value Work: 0.149 
  • R-Value Observed: 0.149 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The mechanism by which a distinguishing arabinofuranosidase can cope with internal di-substitutions in arabinoxylans.

Dos Santos, C.R.de Giuseppe, P.O.de Souza, F.H.M.Zanphorlin, L.M.Domingues, M.N.Pirolla, R.A.S.Honorato, R.V.Tonoli, C.C.C.de Morais, M.A.B.de Matos Martins, V.P.Fonseca, L.M.Buchli, F.de Oliveira, P.S.L.Gozzo, F.C.Murakami, M.T.

(2018) Biotechnol Biofuels 11: 223-223

  • DOI: https://doi.org/10.1186/s13068-018-1212-y
  • Primary Citation of Related Structures:  
    6D25

  • PubMed Abstract: 

    Arabinoxylan is an abundant polysaccharide in industrially relevant biomasses such as sugarcane, corn stover and grasses. However, the arabinofuranosyl di-substitutions that decorate the xylan backbone are recalcitrant to most known arabinofuranosidases (Abfs).


  • Organizational Affiliation

    1Brazilian Bioethanol Science and Technology Laboratory (CTBE), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Sao Paulo 13083-970 Brazil.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha-L-arabinosidase
A, B, C, D, E
A, B, C, D, E, F
520Xanthomonas citri pv. citri str. 306Mutation(s): 0 
Gene Names: XAC1286
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.91 Å
  • R-Value Free: 0.167 
  • R-Value Work: 0.149 
  • R-Value Observed: 0.149 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 91.344α = 90
b = 163.231β = 107.57
c = 114.425γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Sao Paulo Research Foundation (FAPESP)Brazil2013/13309-0, 2014/07135-1 , 2015/26982-0

Revision History  (Full details and data files)

  • Version 1.0: 2019-02-20
    Type: Initial release
  • Version 1.1: 2020-01-01
    Changes: Author supporting evidence
  • Version 1.2: 2023-10-04
    Changes: Data collection, Database references, Refinement description