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PDBsum entry 3nj3

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3nj3
Jmol
Contents
Protein chains
327 a.a.
Ligands
ACT ×2
SO4 ×4
XYP-XYP ×2
Waters ×337
PDB id:
3nj3
Name: Hydrolase
Title: Crystal structure of xylanase 10b from thermotoga petrophila complex with xylobiose
Structure: Endo-1,4-beta-xylanase. Chain: a, b. Fragment: unp residues 21 to 344. Engineered: yes
Source: Thermotoga petrophila rku-1. Organism_taxid: 390874. Strain: rku-1. Gene: tpet_0854. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.88Å     R-factor:   0.234     R-free:   0.299
Authors: C.R.Santos,A.N.Meza,D.M.Trindade,R.Ruller,F.M.Squina,R.A.Pra M.T.Murakami
Key ref: C.R.Santos et al. (2010). Thermal-induced conformational changes in the product release area drive the enzymatic activity of xylanases 10B: Crystal structure, conformational stability and functional characterization of the xylanase 10B from Thermotoga petrophila RKU-1. Biochem Biophys Res Commun, 403, 214-219. PubMed id: 21070746 DOI: 10.1016/j.bbrc.2010.11.010
Date:
16-Jun-10     Release date:   04-May-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
A5IL00  (A5IL00_THEP1) -  Endo-1,4-beta-xylanase
Seq:
Struc:
347 a.a.
327 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 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.bbrc.2010.11.010 Biochem Biophys Res Commun 403:214-219 (2010)
PubMed id: 21070746  
 
 
Thermal-induced conformational changes in the product release area drive the enzymatic activity of xylanases 10B: Crystal structure, conformational stability and functional characterization of the xylanase 10B from Thermotoga petrophila RKU-1.
C.R.Santos, A.N.Meza, Z.B.Hoffmam, J.C.Silva, T.M.Alvarez, R.Ruller, G.M.Giesel, H.Verli, F.M.Squina, R.A.Prade, M.T.Murakami.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21352806 J.Cota, T.M.Alvarez, A.P.Citadini, C.R.Santos, M.de Oliveira Neto, R.R.Oliveira, G.M.Pastore, R.Ruller, R.A.Prade, M.T.Murakami, and F.M.Squina (2011).
Mode of operation and low-resolution structure of a multi-domain and hyperthermophilic endo-β-1,3-glucanase from Thermotoga petrophila.
  Biochem Biophys Res Commun, 406, 590-594.  
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