PDBsum entry 1tax

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protein links
Hydrolase PDB id
Protein chain
302 a.a.
Waters ×165
Superseded by: 1gok 1gok
PDB id:
Name: Hydrolase
Title: Thermostable xylanase i from thermoascus aurantiacus
Structure: Endo-1,4-beta-xylanase. Chain: a. Ec:
Source: Thermoascus aurantiacus. Cellular_location: extracellular
1.14Å     R-factor:   0.180     R-free:   0.201
Authors: L.Lo Leggio,R.W.Pickersgill
Key ref:
L.Lo Leggio et al. (1999). High resolution structure and sequence of T. aurantiacus xylanase I: implications for the evolution of thermostability in family 10 xylanases and enzymes with (beta)alpha-barrel architecture. Proteins, 36, 295-306. PubMed id: 10409823 DOI: 10.1002/(SICI)1097-0134(19990815)36:3<295::AID-PROT4>3.3.CO;2-Y
15-Sep-98     Release date:   16-Sep-99    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P23360  (XYNA_THEAU) -  Endo-1,4-beta-xylanase
329 a.a.
302 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 11 residue positions (black crosses)

 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: 10.1002/(SICI)1097-0134(19990815)36:3<295::AID-PROT4>3.3.CO;2-Y Proteins 36:295-306 (1999)
PubMed id: 10409823  
High resolution structure and sequence of T. aurantiacus xylanase I: implications for the evolution of thermostability in family 10 xylanases and enzymes with (beta)alpha-barrel architecture.
L.Lo Leggio, S.Kalogiannis, M.K.Bhat, R.W.Pickersgill.
Xylanase I is a thermostable xylanase from the fungus Thermoascus aurantiacus, which belongs to family 10 in the current classification of glycosyl hydrolases. We have determined the three-dimensional X-ray structure of this enzyme to near atomic resolution (1.14 A) by molecular replacement, and thereby corrected the chemically determined sequence previously published. Among the five members of family 10 enzymes for which the structure has been determined, Xylanase I from T. aurantiacus and Xylanase Z from C. thermocellum are from thermophilic organisms. A comparison with the three other available structures of the family 10 xylanases from mesophilic organisms suggests that thermostability is effected mainly by improvement of the hydrophobic packing, favorable interactions of charged side chains with the helix dipoles and introduction of prolines at the N-terminus of helices. In contrast to other classes of proteins, there is very little evidence for a contribution of salt bridges to thermostability in the family 10 xylanases from thermophiles. Further analysis of the structures of other proteins from thermophiles with eight-fold (beta)alpha-barrel architecture suggests that favorable interactions of charged side chains with the helix dipoles may be a common way in which thermophilic proteins with this fold are stabilized. As this is the most common type of protein architecture, this finding may provide a useful guide for site-directed mutagenesis aimed to improve the thermostability of (beta)alpha-barrel proteins. Proteins 1999;36:295-306.
  Selected figure(s)  
Figure 2.
Figure 2. Comparison of the structures of TAX, XYLA and XYNZ in a region containing a hydrophobic cavity in XYLA. A hydrophobic cavity present in XYLA (a) is filled by Phe 18 in TAX (b), and by Met 780, Phe 792, and Met 794 in XYNZ (c). The XYLA cavity is shown as a blue net. The figure was produced with QUANTA using the cavity definition of GRASP.
Figure 5.
Figure 5. Stereo representations of typical final electron density maps for the two crystal forms. Two SIGMAA weighted 2F[obs] - F[calc] electron density maps are shown at 1.2 contour level, showing typical final density for the Form I crystal at 1.92 Å resolution a) and for the Form II crystal at 1.14 Å resolution b). The same region of the protein is shown in both views.
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (1999, 36, 295-306) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19940147 O.Gallardo, F.I.Pastor, J.Polaina, P.Diaz, R.Łysek, P.Vogel, P.Isorna, B.González, and J.Sanz-Aparicio (2010).
Structural insights into the specificity of Xyn10B from Paenibacillus barcinonensis and its improved stability by forced protein evolution.
  J Biol Chem, 285, 2721-2733.
PDB codes: 3emc 3emq 3emz
19854928 S.Anbarasan, J.Jänis, M.Paloheimo, M.Laitaoja, M.Vuolanto, J.Karimäki, P.Vainiotalo, M.Leisola, and O.Turunen (2010).
Effect of glycosylation and additional domains on the thermostability of a family 10 xylanase produced by Thermopolyspora flexuosa.
  Appl Environ Microbiol, 76, 356-360.  
  18931429 N.N.Smith, and D.T.Gallagher (2008).
Structure and lability of archaeal dehydroquinase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 886-892.
PDB code: 2ox1
17766385 R.A.Goldstein (2007).
Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: insights from the quasi-chemical approximation.
  Protein Sci, 16, 1887-1895.  
16287076 A.Corazza, C.Rosano, K.Pagano, V.Alverdi, G.Esposito, C.Capanni, F.Bemporad, G.Plakoutsi, M.Stefani, F.Chiti, S.Zuccotti, M.Bolognesi, and P.Viglino (2006).
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus.
  Proteins, 62, 64-79.
PDB codes: 1y9o 2bjd 2bje
15765251 M.K.Ali, F.B.Rudolph, and G.N.Bennett (2005).
Characterization of thermostable Xyn10A enzyme from mesophilic Clostridium acetobutylicum ATCC 824.
  J Ind Microbiol Biotechnol, 32, 12-18.  
15652973 T.Collins, C.Gerday, and G.Feller (2005).
Xylanases, xylanase families and extremophilic xylanases.
  FEMS Microbiol Rev, 29, 3.  
15103129 A.Teplitsky, A.Mechaly, V.Stojanoff, G.Sainz, G.Golan, H.Feinberg, R.Gilboa, V.Reiland, G.Zolotnitsky, D.Shallom, A.Thompson, Y.Shoham, and G.Shoham (2004).
Structure determination of the extracellular xylanase from Geobacillus stearothermophilus by selenomethionyl MAD phasing.
  Acta Crystallogr D Biol Crystallogr, 60, 836-848.
PDB code: 1hiz
14668328 G.Pell, E.J.Taylor, T.M.Gloster, J.P.Turkenburg, C.M.Fontes, L.M.Ferreira, T.Nagy, S.J.Clark, G.J.Davies, and H.J.Gilbert (2004).
The mechanisms by which family 10 glycoside hydrolases bind decorated substrates.
  J Biol Chem, 279, 9597-9605.
PDB codes: 1uqy 1uqz 1ur1 1ur2
14670951 G.Pell, L.Szabo, S.J.Charnock, H.Xie, T.M.Gloster, G.J.Davies, and H.J.Gilbert (2004).
Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases.
  J Biol Chem, 279, 11777-11788.
PDB codes: 1us2 1us3
12761390 J.Le Nours, C.Ryttersgaard, L.Lo Leggio, P.R.Østergaard, T.V.Borchert, L.L.Christensen, and S.Larsen (2003).
Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum.
  Protein Sci, 12, 1195-1204.
PDB codes: 1hjq 1hjs 1hju
11223515 S.Teixeira, L.Lo Leggio, R.Pickersgill, and C.Cardin (2001).
Anisotropic refinement of the structure of Thermoascus aurantiacus xylanase I.
  Acta Crystallogr D Biol Crystallogr, 57, 385-392.
PDB code: 1fxm
11025547 L.L.Leggio, J.Jenkins, G.W.Harris, and R.W.Pickersgill (2000).
X-ray crystallographic study of xylopentaose binding to Pseudomonas fluorescens xylanase A.
  Proteins, 41, 362-373.
PDB code: 1e5n
10974122 R.Maheshwari, G.Bharadwaj, and M.K.Bhat (2000).
Thermophilic fungi: their physiology and enzymes.
  Microbiol Mol Biol Rev, 64, 461-488.  
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 codes are shown on the right.