PDBsum entry 1igo

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Hydrolase PDB id
Protein chains
205 a.a. *
Waters ×109
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Family 11 xylanase
Structure: Family 11 xylanase. Chain: a, b. Synonym: endo-1,4-beta xylanase, family g xylanase. Ec:
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: b230
2.20Å     R-factor:   0.208     R-free:   0.272
Authors: A.J.Oakley,C.Thomson,T.Heinrich,R.Dunlop,M.C.J.Wilce
Key ref:
A.J.Oakley et al. (2003). Characterization of a family 11 xylanase from Bacillus subtillis B230 used for paper bleaching. Acta Crystallogr D Biol Crystallogr, 59, 627-636. PubMed id: 12657781 DOI: 10.1107/S0907444903001227
18-Apr-01     Release date:   18-Apr-02    
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Protein chains
Pfam   ArchSchema ?
Q7SID8  (Q7SID8_BACIU) -  Endo-1,4-beta-xylanase
205 a.a.
205 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.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   3 terms 
  Biochemical function     hydrolase activity     4 terms  


DOI no: 10.1107/S0907444903001227 Acta Crystallogr D Biol Crystallogr 59:627-636 (2003)
PubMed id: 12657781  
Characterization of a family 11 xylanase from Bacillus subtillis B230 used for paper bleaching.
A.J.Oakley, T.Heinrich, C.A.Thompson, M.C.Wilce.
Enzymes such as family 11 xylanases are increasingly being used for industrial applications. Here, the cloning, structure determination and temperature-stability data of a family 11 xylanase, Xyn11X, from the alkali-tolerant Bacillus subtilis subspecies B230 are reported. This enzyme, which degrades xylan polymers, is being produced on an industrial scale for use in the paper-bleaching industry. Xyn11X adopts the canonical family 11 xylanase fold. It has a greater abundance of side chain to side chain hydrogen bonds compared with all other family 11 xylanase crystal structures. Means by which the thermostability of Xyn11X might be improved are suggested.
  Selected figure(s)  
Figure 3.
Figure 3 Structure-based sequence alignment of representative family 11 xylanases. T. reesei, Trichoderma reesei xylanase I (PDB code 1ynx ); A. kawachii, xylanase C from Aspergillus kawachii (1bk1 ); A. niger, Aspergillus niger xylanase I (1ukr ); B. circulans, Bacillus circulans xylanase (1xnb ); T. lanuginosus, Thermomyces lanuginosus xylanase (1yna ); P. variotii, Paecilomyces variotii xylanase (1pvx ); T. harzianum, Trichoderma harzianum xylanase (1xnd ); T. reesei II, Trichoderma reesei xylanase II (1enx ); D. thermophilum, Dictyoglomus thermophilum xylanase (1f5j ); B. subtilis B230, the subject xylanase of the current study; B. agaradhaerens, Bacillus agaradhaerens xylanase (1qh6 ); S. sp. S38, Streptomyces sp. S38 (1hix ). Residues that show structural similarity (P[ij] > 0.5) are capitalized. The catalytic acidic residues are indicated with an asterisk), with the catalytic tyrosine residues indicated (O). Other crucial active-site residues are also indicated (^). The secondary structure as determined by DSSP for Xyn11X is shown above the sequences. Sheet A is coloured cyan. Sheet B is coloured green. The -helix is indicated in red. The amino acids A, F, M, I, L, V, W and Y are coloured yellow, Q, N, S and T are coloured green, E and D are coloured red, H, K, and R are blue and P, G and C are white.
Figure 5.
Figure 5 (a) CD spectra of Xyn11X. (b) CD at 217 nm measured at 1 K intervals.
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 627-636) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19838860 H.Kui, H.Luo, P.Shi, Y.Bai, T.Yuan, Y.Wang, P.Yang, S.Dong, and B.Yao (2010).
Gene cloning, expression, and characterization of a thermostable xylanase from Nesterenkonia xinjiangensis CCTCC AA001025.
  Appl Biochem Biotechnol, 162, 953-965.  
18802693 A.Manimaran, K.S.Kumar, K.Permaul, and S.Singh (2009).
Hyper production of cellulase-free xylanase by Thermomyces lanuginosus SSBP on bagasse pulp and its application in biobleaching.
  Appl Microbiol Biotechnol, 81, 887-893.  
17712584 A.Manimaran, and T.M.Vatsala (2007).
Biobleaching of banana fibre pulp using Bacillus subtilis C O1 xylanase produced from wheat bran under solid-state cultivation.
  J Ind Microbiol Biotechnol, 34, 745-749.  
16652352 M.Kozak (2006).
Solution scattering studies of conformation stability of xylanase XYNII from Trichoderma longibrachiatum.
  Biopolymers, 83, 95.  
  16510999 M.T.Murakami, R.Ruller, R.J.Ward, and R.K.Arni (2005).
Crystallization and preliminary X-ray crystallographic studies of the mesophilic xylanase A from Bacillus subtilis 1A1.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 219-220.  
15652973 T.Collins, C.Gerday, and G.Feller (2005).
Xylanases, xylanase families and extremophilic xylanases.
  FEMS Microbiol Rev, 29, 3.  
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.