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protein ligands metals Protein-protein interface(s) links
Protein binding PDB id
3e4b
Jmol
Contents
Protein chains
395 a.a. *
316 a.a. *
Ligands
GOL ×4
Metals
_CL ×3
Waters ×853
* Residue conservation analysis
PDB id:
3e4b
Name: Protein binding
Title: Crystal structure of algk from pseudomonas fluorescens wcs37
Structure: Algk. Chain: a, b, c, d. Engineered: yes. Mutation: yes
Source: Pseudomonas fluorescens. Organism_taxid: 294. Strain: wcs374r. Gene: algk. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.220     R-free:   0.280
Authors: C.-L.Keiski,M.Harwich,S.Jain,A.M.Neculai,P.Yip,H.Robinson, J.C.Whitney,L.L.Burrows,D.E.Ohman,P.L.Howell
Key ref: C.L.Keiski et al. (2010). AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin. Structure, 18, 265-273. PubMed id: 20159471 DOI: 10.1016/j.str.2009.11.015
Date:
11-Aug-08     Release date:   25-Aug-09    
PROCHECK
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 Headers
 References

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     binding     1 term  

 

 
DOI no: 10.1016/j.str.2009.11.015 Structure 18:265-273 (2010)
PubMed id: 20159471  
 
 
AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin.
C.L.Keiski, M.Harwich, S.Jain, A.M.Neculai, P.Yip, H.Robinson, J.C.Whitney, L.Riley, L.L.Burrows, D.E.Ohman, P.L.Howell.
 
  ABSTRACT  
 
The opportunistic pathogen Pseudomonas aeruginosa causes chronic biofilm infections in cystic fibrosis patients. During colonization of the lung, P. aeruginosa converts to a mucoid phenotype characterized by overproduction of the exopolysaccharide alginate. Here we show that AlgK, a protein essential for production of high molecular weight alginate, is an outer membrane lipoprotein that contributes to the correct localization of the porin AlgE. Our 2.5 A structure shows AlgK is composed of 9.5 tetratricopeptide-like repeats, and three putative sites of protein-protein interaction have been identified. Bioinformatics analysis suggests that BcsA, PgaA, and PelB, involved in the production and export of cellulose, poly-beta-1,6-N-Acetyl-D-glucosamine, and Pel exopolysaccharide, respectively, share the same topology as AlgK/E. Together, our data suggest that AlgK plays a role in the assembly of the alginate biosynthetic complex and represents the periplasmic component of a new type of outer membrane secretin that differs from canonical bacterial capsular polysaccharide secretion systems.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20159460 C.Whitfield, and I.L.Mainprize (2010).
TPR motifs: hallmarks of a new polysaccharide export scaffold.
  Structure, 18, 151-153.  
  20445266 J.T.Weadge, P.P.Yip, H.Robinson, K.Arnett, P.A.Tipton, and P.L.Howell (2010).
Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 588-591.  
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