PDBsum entry 1jjf

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protein metals links
Hydrolase PDB id
Protein chain
255 a.a. *
Waters ×281
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase z of clostridium thermocellum
Structure: Endo-1,4-beta-xylanase z. Chain: a. Fragment: residues 20-287. Synonym: feruloyl esterase. Xylanase z. 1,4-beta-d-xylan xylanohydrolase z. Engineered: yes
Source: Clostridium thermocellum. Organism_taxid: 1515. Gene: xynz. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
1.75Å     R-factor:   0.189     R-free:   0.206
Authors: F.D.Schubot,I.A.Kataeva,D.L.Blum,A.K.Shah,L.G.Ljungdahl, J.P.Rose,B.C.Wang,Southeast Collaboratory For Structural Genomics (Secsg)
Key ref:
F.D.Schubot et al. (2001). Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum. Biochemistry, 40, 12524-12532. PubMed id: 11601976 DOI: 10.1021/bi011391c
05-Jul-01     Release date:   31-Oct-01    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P10478  (XYNZ_CLOTH) -  Endo-1,4-beta-xylanase Z
837 a.a.
255 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Endo-1,4-beta-xylanase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.


DOI no: 10.1021/bi011391c Biochemistry 40:12524-12532 (2001)
PubMed id: 11601976  
Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum.
F.D.Schubot, I.A.Kataeva, D.L.Blum, A.K.Shah, L.G.Ljungdahl, J.P.Rose, B.C.Wang.
Feruloyl esterases function in the cleavage of ferulic acid's bonds to arabinoxylan and pectin where the ferulic acid moieties cross-link the layers of polysaccharide chains within hemicellulose. This work presents the crystal structure of FAE_XynZ, the domain of Clostridium thermocellum's cellulosomal xylanase Z that displays feruloyl esterase activity. The structure was obtained via multiple isomorphous replacement with anomalous scattering (MIRAS) using three heavy atom derivatives and refined against X-ray diffraction data of up to 1.75 A resolution. The R-value of the final model was 0.187 (R(free) = 0.21). FAE_XynZ displays an eight-stranded alpha/beta-fold with the characteristic "catalytic triad" at the heart of the active site. To define the substrate specificity determinants of the enzyme, the crystal structures of FAE_XynZ and the inactive FAE_XynZ(S172A) mutant were determined in complexes with the feruloyl-arabinoxylans FAXX and FAX(3), respectively. In the complex crystals, the ferulic acid moieties are clearly recognizable and allowed identification of the hydrophobic binding pocket. The carbohydrate part of both substrates is not visible in either structure. The location of the putative carbohydrate binding-pocket was inferred based on the location and orientation of the adjacent ferulic acid molecule. Five of the six residues lining the pocket were found to be conserved in FAE A from Orpinomyces sp., which further supports the proposed role of these amino acids.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21362116 M.Qi, P.Wang, L.B.Selinger, L.J.Yanke, R.J.Forster, and T.A.McAllister (2011).
Isolation and characterization of a ferulic acid esterase (Fae1A) from the rumen fungus Anaeromyces mucronatus.
  J Appl Microbiol, 110, 1341-1350.  
19304844 D.Dodd, S.A.Kocherginskaya, M.A.Spies, K.E.Beery, C.A.Abbas, R.I.Mackie, and I.K.Cann (2009).
Biochemical analysis of a beta-D-xylosidase and a bifunctional xylanase-ferulic acid esterase from a xylanolytic gene cluster in Prevotella ruminicola 23.
  J Bacteriol, 191, 3328-3338.  
19644688 T.Koseki, S.Fushinobu, Ardiansyah, H.Shirakawa, and M.Komai (2009).
Occurrence, properties, and applications of feruloyl esterases.
  Appl Microbiol Biotechnol, 84, 803-810.  
18378601 L.G.Ljungdahl (2008).
The cellulase/hemicellulase system of the anaerobic fungus Orpinomyces PC-2 and aspects of its applied use.
  Ann N Y Acad Sci, 1125, 308-321.  
17932928 M.H.Kim, B.S.Kang, S.Kim, K.J.Kim, C.H.Lee, B.C.Oh, S.C.Park, and T.K.Oh (2008).
The crystal structure of the estA protein, a virulence factor from Streptococcus pneumoniae.
  Proteins, 70, 578-583.
PDB code: 2uz0
17989872 A.E.Fazary, and Y.H.Ju (2007).
Feruloyl esterases as biotechnological tools: current and future perspectives.
  Acta Biochim Biophys Sin (Shanghai), 39, 811-828.  
16431911 E.J.Taylor, T.M.Gloster, J.P.Turkenburg, F.Vincent, A.M.Brzozowski, C.Dupont, F.Shareck, M.S.Centeno, J.A.Prates, V.Puchart, L.M.Ferreira, C.M.Fontes, P.Biely, and G.J.Davies (2006).
Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases.
  J Biol Chem, 281, 10968-10975.
PDB codes: 2c71 2c79 2cc0
16320365 S.W.Hinz, C.H.Doeswijk-Voragen, R.Schipperus, L.A.van den Broek, J.P.Vincken, and A.G.Voragen (2006).
Increasing the transglycosylation activity of alpha-galactosidase from Bifidobacterium adolescentis DSM 20083 by site-directed mutagenesis.
  Biotechnol Bioeng, 93, 122-131.  
16128806 C.B.Faulds, R.Molina, R.Gonzalez, F.Husband, N.Juge, J.Sanz-Aparicio, and J.A.Hermoso (2005).
Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger.
  FEBS J, 272, 4362-4371.
PDB code: 2bjh
15103133 K.E.McAuley, A.Svendsen, S.A.Patkar, and K.S.Wilson (2004).
Structure of a feruloyl esterase from Aspergillus niger.
  Acta Crystallogr D Biol Crystallogr, 60, 878-887.
PDB codes: 1uwc 1uza
12831897 D.Shallom, and Y.Shoham (2003).
Microbial hemicellulases.
  Curr Opin Microbiol, 6, 219-228.  
11738044 J.A.Prates, N.Tarbouriech, S.J.Charnock, C.M.Fontes, L.M.Ferreira, and G.J.Davies (2001).
The structure of the feruloyl esterase module of xylanase 10B from Clostridium thermocellum provides insights into substrate recognition.
  Structure, 9, 1183-1190.
PDB codes: 1gkk 1gkl
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.