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PDBsum entry 4c24

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protein ligands metals links
Lyase PDB id
4c24
Jmol
Contents
Protein chain
211 a.a.
Ligands
SO4 ×2
EDO
GOL
Metals
_ZN
_NI
Waters ×102
PDB id:
4c24
Name: Lyase
Title: L-fuculose 1-phosphate aldolase
Structure: L-fuculose phosphate aldolase. Chain: a. Synonym: l-fuculose 1-phosphate aldolase. Engineered: yes
Source: Streptococcus pneumoniae. Organism_taxid: 170187. Strain: tigr4. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.50Å     R-factor:   0.140     R-free:   0.160
Authors: M.A.Higgins,M.D.L.Suits,C.Marsters,A.B.Boraston
Key ref: M.A.Higgins et al. (2014). Structural and functional analysis of fucose-processing enzymes from Streptococcus pneumoniae. J Mol Biol, 426, 1469-1482. PubMed id: 24333485 DOI: 10.1016/j.jmb.2013.12.006
Date:
16-Aug-13     Release date:   11-Dec-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q97N89  (Q97N89_STRPN) -  L-fuculose phosphate aldolase
Seq:
Struc:
212 a.a.
211 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.4.1.2.17  - L-fuculose-phosphate aldolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
L-fuculose 1-phosphate
= glycerone phosphate
+
(S)-lactaldehyde
Bound ligand (Het Group name = GOL)
matches with 83.33% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     lyase activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.jmb.2013.12.006 J Mol Biol 426:1469-1482 (2014)
PubMed id: 24333485  
 
 
Structural and functional analysis of fucose-processing enzymes from Streptococcus pneumoniae.
M.A.Higgins, M.D.Suits, C.Marsters, A.B.Boraston.
 
  ABSTRACT  
 
Fucose metabolism pathways are present in many bacterial species and typically contain the central fucose-processing enzymes fucose isomerase (FcsI), fuculose kinase (FcsK), and fuculose-1-phosphate aldolase (FcsA). Fucose initially undergoes isomerization by FcsI producing fuculose, which is then phosphorylated by FcsK. FcsA cleaves the fuculose-1-phosphate product into lactaldehyde and dihydroxyacetone phosphate, which can be incorporated into central metabolism allowing the bacterium to use fucose as an energy source. Streptococcus pneumoniae has fucose-processing operons containing homologs of FcsI, FcsK, and FcsA; however, this bacterium appears unable to utilize fucose as an energy source. To investigate this contradiction, we performed biochemical and structural studies of the S. pneumoniae fucose-processing enzymes SpFcsI, SpFcsK, and SpFcsA. These enzymes are demonstrated to act in a sequential manner to ultimately produce dihydroxyacetone phosphate and have structural features entirely consistent with their observed biochemical activities. Analogous to the regulation of the Escherichia coli fucose utilization operon, fuculose-1-phosphate appears to act as an inducing molecule for activation of the S. pneumoniae fucose operon. Despite our evidence that S. pneumoniae appears to have the appropriate regulatory and biochemical machinery for fucose metabolism, we confirmed the inability of the S. pneumoniae TIGR4 strain to grow on fucose or on the H-disaccharide, which is the probable substrate of the transporter for the pathway. On the basis of these observations, we postulate that the S. pneumoniae fucose-processing pathway has a non-metabolic role in the interaction of this bacterium with its human host.