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PDBsum entry 3rdk

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3rdk
Jmol
Contents
Protein chains
333 a.a.
Ligands
GCV-XYP-XYP-XYS ×2
GOL ×9
Metals
_MG
_CL ×3
Waters ×723
PDB id:
3rdk
Name: Hydrolase
Title: Protein crystal structure of xylanase a1 of paenibacillus sp
Structure: Endo-1,4-beta-xylanase. Chain: a, b. Fragment: catalytic domain. Engineered: yes
Source: Paenibacillus sp. Jdr-2. Organism_taxid: 324057. Strain: jdr-2. Gene: pjdr2_0221. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.49Å     R-factor:   0.147     R-free:   0.184
Authors: E.Pozharski,F.J.St John
Key ref: F.J.St John et al. (2012). Novel structural features of xylanase A1 from Paenibacillus sp. JDR-2. J Struct Biol, 180, 303-311. PubMed id: 23000703 DOI: 10.1016/j.jsb.2012.09.007
Date:
01-Apr-11     Release date:   04-Apr-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
C6CRV0  (XYNA1_PAESJ) -  Endo-1,4-beta-xylanase A
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1462 a.a.
333 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     carbohydrate metabolic process   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term  

 

 
DOI no: 10.1016/j.jsb.2012.09.007 J Struct Biol 180:303-311 (2012)
PubMed id: 23000703  
 
 
Novel structural features of xylanase A1 from Paenibacillus sp. JDR-2.
F.J.St John, J.F.Preston, E.Pozharski.
 
  ABSTRACT  
 
The Gram-positive bacterium Paenibacillus sp. JDR-2 (PbJDR2) has been shown to have novel properties in the utilization of the abundant but chemically complex hemicellulosic sugar glucuronoxylan. Xylanase A1 of PbJDR2 (PbXynA1) has been implicated in an efficient process in which extracellular depolymerization of this polysaccharide is coupled to assimilation and intracellular metabolism. PbXynA1is a 154kDa cell wall anchored multimodular glycosyl hydrolase family 10 (GH10) xylanase. In this work, the 38kDa catalytic module of PbXynA1 has been structurally characterized revealing several new features not previously observed in structures of GH10 xylanases. These features are thought to facilitate hydrolysis of highly substituted, chemically complex xylans that may be the form found in close proximity to the cell wall of PbJDR2, an organism shown to have a preference for growth on polymeric glucuronoxylan.
 

 

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