spacer
spacer
Go to PDB code: 
protein ligands links
Hydrolase PDB id
1xxn
Jmol
Contents
Protein chain
185 a.a. *
Ligands
SRT
Waters ×145
* Residue conservation analysis
PDB id:
1xxn
Name: Hydrolase
Title: Crystal structure of a mesophilic xylanase a from bacillus subtilis 1a1
Structure: Endo-1,4-beta-xylanase a. Chain: a. Synonym: xylanase a, 1,4-beta-d-xylan xylanohydrolase a. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: 1a1. Gene: xyna. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
1.70Å     R-factor:   0.173     R-free:   0.212
Authors: M.T.Murakami,R.Ruller,R.J.Ward,R.K.Arni
Key ref: M.T.Murakami et al. (2005). Correlation of temperature induced conformation change with optimum catalytic activity in the recombinant G/11 xylanase A from Bacillus subtilis strain 168 (1A1). Febs Lett, 579, 6505-6510. PubMed id: 16289057 DOI: 10.1016/j.febslet.2005.10.039
Date:
07-Nov-04     Release date:   18-Oct-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P18429  (XYNA_BACSU) -  Endo-1,4-beta-xylanase A
Seq:
Struc: 		213 a.a.
185 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.8  - 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: 10.1016/j.febslet.2005.10.039 Febs Lett 579:6505-6510 (2005)
PubMed id: 16289057  
 
 
Correlation of temperature induced conformation change with optimum catalytic activity in the recombinant G/11 xylanase A from Bacillus subtilis strain 168 (1A1).
M.T.Murakami, R.K.Arni, D.S.Vieira, L.Degrève, R.Ruller, R.J.Ward.
 
  ABSTRACT  
 
The 1.7A resolution crystal structure of recombinant family G/11 beta-1,4-xylanase (rXynA) from Bacillus subtilis 1A1 shows a jellyroll fold in which two curved beta-sheets form the active-site and substrate-binding cleft. The onset of thermal denaturation of rXynA occurs at 328 K, in excellent agreement with the optimum catalytic temperature. Molecular dynamics simulations at temperatures of 298-328 K demonstrate that below the optimum temperature the thumb loop and palm domain adopt a closed conformation. However, at 328 K these two domains separate facilitating substrate access to the active-site pocket, thereby accounting for the optimum catalytic temperature of the rXynA.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20225927 A.Pollet, J.A.Delcour, and C.M.Courtin (2010).
Structural determinants of the substrate specificities of xylanases from different glycoside hydrolase families.
  Crit Rev Biotechnol, 30, 176-191.  
19422059 A.Pollet, E.Vandermarliere, J.Lammertyn, S.V.Strelkov, J.A.Delcour, and C.M.Courtin (2009).
Crystallographic and activity-based evidence for thumb flexibility and its relevance in glycoside hydrolase family 11 xylanases.
  Proteins, 77, 395-403.
PDB code: 3exu
17876824 R.Ruller, L.Deliberto, T.L.Ferreira, and R.J.Ward (2008).
Thermostable variants of the recombinant xylanase A from Bacillus subtilis produced by directed evolution show reduced heat capacity changes.
  Proteins, 70, 1280-1293.  
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.