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PDBsum entry 1ald

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protein links
Lyase (aldehyde) PDB id
1ald
Jmol
Contents
Protein chain
363 a.a. *
* Residue conservation analysis
PDB id:
1ald
Name: Lyase (aldehyde)
Title: Activity and specificity of human aldolases
Structure: Aldolase a. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Biol. unit: Tetramer (from PQS)
Resolution:
2.00Å     R-factor:   0.220    
Authors: H.C.Watson
Key ref: S.J.Gamblin et al. (1991). Activity and specificity of human aldolases. J Mol Biol, 219, 573-576. PubMed id: 2056525
Date:
05-May-91     Release date:   15-Jan-92    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04075  (ALDOA_HUMAN) -  Fructose-bisphosphate aldolase A
Seq:
Struc:
364 a.a.
363 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.1.2.13  - Fructose-bisphosphate aldolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
= glycerone phosphate
+ D-glyceraldehyde 3-phosphate
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   11 terms 
  Biological process     small molecule metabolic process   16 terms 
  Biochemical function     catalytic activity     10 terms  

 

 
    reference    
 
 
J Mol Biol 219:573-576 (1991)
PubMed id: 2056525  
 
 
Activity and specificity of human aldolases.
S.J.Gamblin, G.J.Davies, J.M.Grimes, R.M.Jackson, J.A.Littlechild, H.C.Watson.
 
  ABSTRACT  
 
The structure of the type I fructose 1,6-bisphosphate aldolase from human muscle has been extended from 3 A to 2 A resolution. The improvement in the resulting electron density map is such that the 20 or so C-terminal residues, known to be associated with activity and isozyme specificity, have been located. The side-chain of the Schiff's base-forming lysine 229 is located towards the centre of an eight-stranded beta-barrel type structure. The C-terminal "tail" extends from the rim of the beta-barrel towards lysine 229, thus forming part of the active site of the enzyme. This structural arrangement appears to explain the difference in activity and specificity of the three tissue-specific human aldolases and helps with our understanding of the type I aldolase reaction mechanism.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20934451 D.W.Song, J.G.Lee, H.S.Youn, S.H.Eom, and d.o. .H.Kim (2011).
Ryanodine receptor assembly: A novel systems biology approach to 3D mapping.
  Prog Biophys Mol Biol, 105, 145-161.  
18652881 Y.Sato, and M.Nishida (2009).
Electric charge divergence in proteins: insights into the evolution of their three-dimensional properties.
  Gene, 441, 3.  
18438970 A.G.Gehring, J.L.Ezzell, and H.G.Lebherz (2008).
A selective reaction of fructose bisphosphate aldolase with fluorescein isothiocyanate in chicken muscle extracts.
  J Mol Recognit, 21, 137-147.  
18676612 I.Kramerova, E.Kudryashova, B.Wu, C.Ottenheijm, H.Granzier, and M.J.Spencer (2008).
Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle.
  Hum Mol Genet, 17, 3271-3280.  
18453690 M.Sherawat, D.R.Tolan, and K.N.Allen (2008).
Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant.
  Acta Crystallogr D Biol Crystallogr, 64, 543-550.
PDB code: 3bv4
17154157 C.A.Buscaglia, W.G.Hol, V.Nussenzweig, and T.Cardozo (2007).
Modeling the interaction between aldolase and the thrombospondin-related anonymous protein, a key connection of the malaria parasite invasion machinery.
  Proteins, 66, 528-537.  
17935305 J.A.Pezza, J.D.Stopa, E.M.Brunyak, K.N.Allen, and D.R.Tolan (2007).
Thermodynamic analysis shows conformational coupling and dynamics confer substrate specificity in fructose-1,6-bisphosphate aldolase.
  Biochemistry, 46, 13010-13018.  
17919319 R.R.Gabdoulline, M.Stein, and R.C.Wade (2007).
qPIPSA: relating enzymatic kinetic parameters and interaction fields.
  BMC Bioinformatics, 8, 373.  
16756667 D.Steinke, S.Hoegg, H.Brinkmann, and A.Meyer (2006).
Three rounds (1R/2R/3R) of genome duplications and the evolution of the glycolytic pathway in vertebrates.
  BMC Biol, 4, 16.  
16705464 P.Y.Cho, M.J.Lee, T.I.Kim, S.Y.Kang, and S.J.Hong (2006).
Expressed sequence tag analysis of adult Clonorchis sinensis, the Chinese liver fluke.
  Parasitol Res, 99, 602-608.  
15537755 T.L.Arakaki, J.A.Pezza, M.A.Cronin, C.E.Hopkins, D.B.Zimmer, D.R.Tolan, and K.N.Allen (2004).
Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function.
  Protein Sci, 13, 3077-3084.
PDB code: 1xfb
11779856 A.Maurady, A.Zdanov, D.de Moissac, D.Beaudry, and J.Sygusch (2002).
A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases.
  J Biol Chem, 277, 9474-9483.
PDB codes: 1ewd 1ewe 1ewg 1ex5 3b8d
11835505 A.P.Zabell, and C.B.Post (2002).
Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints.
  Proteins, 46, 295-307.  
11796620 J.S.McCarthy, M.Wieseman, J.Tropea, D.Kaslow, D.Abraham, S.Lustigman, R.Tuan, R.H.Guderian, and T.B.Nutman (2002).
Onchocerca volvulus glycolytic enzyme fructose-1,6-bisphosphate aldolase as a target for a protective immune response in humans.
  Infect Immun, 70, 851-858.  
11679716 A.R.Dalby, D.R.Tolan, and J.A.Littlechild (2001).
The structure of human liver fructose-1,6-bisphosphate aldolase.
  Acta Crystallogr D Biol Crystallogr, 57, 1526-1533.
PDB code: 1qo5
11512153 C.L.Verlinde, V.Hannaert, C.Blonski, M.Willson, J.J.Périé, L.A.Fothergill-Gilmore, F.R.Opperdoes, M.H.Gelb, W.G.Hol, and P.A.Michels (2001).
Glycolysis as a target for the design of new anti-trypanosome drugs.
  Drug Resist Updat, 4, 50-65.  
  10048322 A.Dalby, Z.Dauter, and J.A.Littlechild (1999).
Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications.
  Protein Sci, 8, 291-297.
PDB codes: 2ald 4ald
  10460186 E.J.Giltay, D.van Schaardenburg, L.J.Gooren, P.J.Kostense, and B.A.Dijkmans (1999).
Decreased serum biochemical markers of muscle origin in patients with ankylosing spondylitis.
  Ann Rheum Dis, 58, 541-545.  
  9610797 M.Ali, P.Rellos, and T.M.Cox (1998).
Hereditary fructose intolerance.
  J Med Genet, 35, 353-365.  
9211740 N.Nikoh, N.Iwabe, K.Kuma, M.Ohno, T.Sugiyama, Y.Watanabe, K.Yasui, Z.Shi-cui, K.Hori, Y.Shimura, and T.Miyata (1997).
An estimate of divergence time of Parazoa and Eumetazoa and that of Cephalochordata and Vertebrata by aldolase and triose phosphate isomerase clocks.
  J Mol Evol, 45, 97.  
9406553 P.T.Erskine, N.Senior, S.Awan, R.Lambert, G.Lewis, I.J.Tickle, M.Sarwar, P.Spencer, P.Thomas, M.J.Warren, P.M.Shoolingin-Jordan, S.P.Wood, and J.B.Cooper (1997).
X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase.
  Nat Struct Biol, 4, 1025-1031.
PDB code: 1aw5
  8935175 A.Dalby, and J.A.Littlechild (1996).
Studies with type I aldolase to understand fructose intolerance and combat parasitic disease.
  J Pharm Pharmacol, 48, 214-217.  
8805555 J.Jia, W.Huang, U.Schörken, H.Sahm, G.A.Sprenger, Y.Lindqvist, and G.Schneider (1996).
Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family.
  Structure, 4, 715-724.
PDB code: 1onr
8636111 J.Wang, A.J.Morris, D.R.Tolan, and L.Pagliaro (1996).
The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants.
  J Biol Chem, 271, 6861-6865.  
8829634 M.Ali, C.L.James, and T.M.Cox (1996).
A newly identified aldolase B splicing mutation (G-->C, 5' intron 5) in hereditary fructose intolerance from New Zealand.
  Hum Mutat, 7, 155-157.  
  8880583 R.Santamaria, S.Tamasi, G.Del Piano, G.Sebastio, G.Andria, C.Borrone, G.Faldella, P.Izzo, and F.Salvatore (1996).
Molecular basis of hereditary fructose intolerance in Italy: identification of two novel mutations in the aldolase B gene.
  J Med Genet, 33, 786-788.  
8939754 S.J.Cooper, G.A.Leonard, S.M.McSweeney, A.W.Thompson, J.H.Naismith, S.Qamar, A.Plater, A.Berry, and W.N.Hunter (1996).
The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold.
  Structure, 4, 1303-1315.
PDB code: 1zen
8535439 D.R.Tolan (1995).
Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene.
  Hum Mutat, 6, 210-218.  
7851430 L.C.Packman, and A.Berry (1995).
A reactive, surface cysteine residue of the class-II fructose-1,6-bisphosphate aldolase of Escherichia coli revealed by electrospray ionisation mass spectrometry.
  Eur J Biochem, 227, 510-515.  
  7849601 W.R.Taylor, T.P.Flores, and C.A.Orengo (1994).
Multiple protein structure alignment.
  Protein Sci, 3, 1858-1870.  
8488556 J.A.Littlechild, and H.C.Watson (1993).
A data-based reaction mechanism for type I fructose bisphosphate aldolase.
  Trends Biochem Sci, 18, 36-39.  
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. Where a reference describes a PDB structure, the PDB code is shown on the right.