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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2vy0
Jmol
Contents
Protein chains
264 a.a. *
Ligands
MPD ×2
MRD ×2
Metals
_CL ×3
_NA ×3
_CA ×2
Waters ×252
* Residue conservation analysis
PDB id:
2vy0
Name: Hydrolase
Title: The x-ray structure of endo-beta-1,3-glucanase from pyrococcus furiosus
Structure: Endo-beta-1,3-glucanase. Chain: a, b. Fragment: residues 35-297. Engineered: yes
Source: Pyrococcus furiosus. Organism_taxid: 2261. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.16Å     R-factor:   0.193     R-free:   0.229
Authors: A.Ilari,A.Fiorillo
Key ref: A.Ilari et al. (2009). Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus- structural basis of substrate recognition. Febs J, 276, 1048-1058. PubMed id: 19154353 DOI: 10.1111/j.1742-4658.2008.06848.x
Date:
15-Jul-08     Release date:   24-Mar-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O73951  (O73951_9EURY) -  Endo-beta-1,3-glucanase (Precursor)
Seq:
Struc: 		297 a.a.
264 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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: 10.1111/j.1742-4658.2008.06848.x Febs J 276:1048-1058 (2009)
PubMed id: 19154353  
 
 
Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus- structural basis of substrate recognition.
A.Ilari, A.Fiorillo, S.Angelaccio, R.Florio, R.Chiaraluce, J.van der Oost, V.Consalvi.
 
  ABSTRACT  
 
Bacterial and archaeal endo-beta-1,3-glucanases that belong to glycoside hydrolase family 16 share a beta-jelly-roll fold, but differ significantly in sequence and in substrate specificity. The crystal structure of the laminarinase (EC 3.2.1.39) from the hyperthermophilic archaeon Pyrococcus furiosus (pfLamA) has been determined at 2.1 A resolution by molecular replacement. The pfLamA structure reveals a kink of six residues (72-77) at the entrance of the catalytic cleft. This peptide is absent in the endoglucanases from alkaliphilic Nocardiopsis sp. strain F96 and Bacillus macerans, two proteins displaying an overall fold similar to that of pfLamA, but with different substrate specificity. A deletion mutant of pfLamA, lacking residues 72-75, hydrolyses the mixed-linkage beta-1,3-1,4-glucan lichenan 10 times more efficiently than the wild-type protein, indicating the importance of the kink in substrate preference.
 

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.  
19769746 J.Vasur, R.Kawai, E.Andersson, K.Igarashi, M.Sandgren, M.Samejima, and J.Ståhlberg (2009).
X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis.
  FEBS J, 276, 3858-3869.  
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.