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PDBsum entry 1cnq

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protein ligands metals links
Hydrolase PDB id
1cnq
Jmol
Contents
Protein chain
332 a.a. *
Ligands
F6P ×2
PO4
Metals
_ZN ×3
Waters ×139
* Residue conservation analysis
PDB id:
1cnq
Name: Hydrolase
Title: Fructose-1,6-bisphosphatase complexed with fructose-6-phosph zinc ions
Structure: Fructose-1,6-bisphosphatase. Chain: a. Synonym: fbpase. Engineered: yes
Source: Sus scrofa. Pig. Organism_taxid: 9823. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PDB file)
Resolution:
2.27Å     R-factor:   0.168     R-free:   0.227
Authors: J.Choe,B.W.Poland,H.Fromm,R.Honzatko
Key ref:
J.Y.Choe et al. (1998). Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase. Biochemistry, 37, 11441-11450. PubMed id: 9708979 DOI: 10.1021/bi981112u
Date:
21-May-99     Release date:   28-May-99    
Supersedes: 1bfl
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00636  (F16P1_PIG) -  Fructose-1,6-bisphosphatase 1
Seq:
Struc:
338 a.a.
332 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.11  - Fructose-bisphosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Pentose Phosphate Pathway (later stages)
      Reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
D-fructose 1,6-bisphosphate
+ H(2)O
=
D-fructose 6-phosphate
Bound ligand (Het Group name = F6P)
corresponds exactly
+
phosphate
Bound ligand (Het Group name = PO4)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     metabolic process   12 terms 
  Biochemical function     catalytic activity     7 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi981112u Biochemistry 37:11441-11450 (1998)
PubMed id: 9708979  
 
 
Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase.
J.Y.Choe, B.W.Poland, H.J.Fromm, R.B.Honzatko.
 
  ABSTRACT  
 
A disordered loop (loop 52-72, residues 52-72) in crystal structures of fructose-1,6-bisphosphatase (FBPase) has been implicated in regulatory and catalytic phenomena by studies in directed mutation. A crystal structure of FBPase in a complex with three zinc cations and the products fructose 6-phosphate (F6P) and phosphate (Pi) reveals loop 52-72 for the first time in a well-defined conformation with strong electron density. Loop 52-57 interacts primarily with the active site of its own subunit. Asp68 of the loop hydrogen bonds with Arg276 and a zinc cation located at the putative potassium activation site. Leu56 and Tyr57 of the loop pack against hydrophobic residues from two separate subunits of FBPase. A mechanism of allosteric regulation of catalysis is presented, in which AMP, by binding to its allosteric pocket, displaces loop 52-72 from the active site. Furthermore, the current structure suggests that both the alpha- and beta-anomers of F6P can be substrates in the reverse reaction catalyzed by FBPase. Mechanisms of catalysis are proposed for the reverse reaction in which Asp121 serves as a catalytic base for the alpha-anomer and Glu280 serves as a catalytic base for the beta-anomer.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18214967 A.Gizak, E.Maciaszczyk, A.Dzugaj, K.Eschrich, and D.Rakus (2008).
Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase.
  Proteins, 72, 209-216.  
17567577 J.K.Hines, C.E.Kruesel, H.J.Fromm, and R.B.Honzatko (2007).
Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch.
  J Biol Chem, 282, 24697-24706.
PDB code: 2q8m
17933867 J.K.Hines, X.Chen, J.C.Nix, H.J.Fromm, and R.B.Honzatko (2007).
Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition.
  J Biol Chem, 282, 36121-36131.
PDB codes: 2qvr 2qvu 2qvv
16670087 J.K.Hines, H.J.Fromm, and R.B.Honzatko (2006).
Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase.
  J Biol Chem, 281, 18386-18393.
PDB code: 2gq1
15858264 R.Gill, F.Mohammed, R.Badyal, L.Coates, P.Erskine, D.Thompson, J.Cooper, M.Gore, and S.Wood (2005).
High-resolution structure of myo-inositol monophosphatase, the putative target of lithium therapy.
  Acta Crystallogr D Biol Crystallogr, 61, 545-555.
PDB code: 2bji
14978036 S.W.Nelson, R.B.Honzatko, and H.J.Fromm (2004).
Origin of cooperativity in the activation of fructose-1,6-bisphosphatase by Mg2+.
  J Biol Chem, 279, 18481-18487.  
12674499 D.Rakus, H.Tillmann, R.Wysocki, S.Ulaszewski, K.Eschrich, and A.Dzugaj (2003).
Different sensitivities of mutants and chimeric forms of human muscle and liver fructose-1,6-bisphosphatases towards AMP.
  Biol Chem, 384, 51-58.  
12595528 J.Y.Choe, C.V.Iancu, H.J.Fromm, and R.B.Honzatko (2003).
Metaphosphate in the active site of fructose-1,6-bisphosphatase.
  J Biol Chem, 278, 16015-16020.
PDB codes: 1nuw 1nux 1nuy
12595529 J.Y.Choe, S.W.Nelson, H.J.Fromm, and R.B.Honzatko (2003).
Interaction of Tl+ with product complexes of fructose-1,6-bisphosphatase.
  J Biol Chem, 278, 16008-16014.
PDB codes: 1nuz 1nv0 1nv1 1nv2 1nv3 1nv4 1nv5 1nv6 1nv7
11741996 Z.Hou, W.Wang, H.J.Fromm, and R.B.Honzatko (2002).
IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli.
  J Biol Chem, 277, 5970-5976.
PDB codes: 1kjx 1kkb 1kkf
11723795 J.Wen, S.W.Nelson, R.B.Honzatko, H.J.Fromm, and J.W.Petrich (2001).
Environment of tryptophan 57 in porcine fructose-1,6-bisphosphatase studied by time-resolved fluorescence and site-directed mutagenesis.
  Photochem Photobiol, 74, 679-685.  
11170378 K.A.Johnson, L.Chen, H.Yang, M.F.Roberts, and B.Stec (2001).
Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities.
  Biochemistry, 40, 618-630.
PDB codes: 1g0h 1g0i
11455598 N.Kelley-Loughnane, and E.R.Kantrowitz (2001).
Binding of AMP to two of the four subunits of pig kidney fructose-1,6-bisphosphatase induces the allosteric transition.
  Proteins, 44, 255-261.  
11451439 N.Kelley-Loughnane, and E.R.Kantrowitz (2001).
AMP inhibition of pig kidney fructose-1,6-bisphosphatase.
  Biochim Biophys Acta, 1548, 66-71.  
10987362 F.W.Zhang, F.K.Zhao, and G.J.Xu (2000).
Molecular cloning, expression and purification of muscle fructose-1,6-bisphosphatase from Zaocys dhumnades: the role of the N-terminal sequence in AMP activation at alkaline pH.
  Biol Chem, 381, 561-566.  
10759847 J.G.Cárcamo, A.J.Yañez, H.C.Ludwig, O.León, R.O.Pinto, A.M.Reyes, and J.C.Slebe (2000).
The C1-C2 interface residue lysine 50 of pig kidney fructose-1, 6-bisphosphatase has a crucial role in the cooperative signal transmission of the AMP inhibition.
  Eur J Biochem, 267, 2242-2251.  
10913263 J.Y.Choe, H.J.Fromm, and R.B.Honzatko (2000).
Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes.
  Biochemistry, 39, 8565-8574.
PDB codes: 1eyi 1eyj 1eyk
10998248 S.W.Nelson, C.V.Iancu, J.Y.Choe, R.B.Honzatko, and H.J.Fromm (2000).
Tryptophan fluorescence reveals the conformational state of a dynamic loop in recombinant porcine fructose-1,6-bisphosphatase.
  Biochemistry, 39, 11100-11106.
PDB codes: 1fj6 1fj9
10581254 M.Chiadmi, A.Navaza, M.Miginiac-Maslow, J.P.Jacquot, and J.Cherfils (1999).
Redox signalling in the chloroplast: structure of oxidized pea fructose-1,6-bisphosphate phosphatase.
  EMBO J, 18, 6809-6815.
PDB codes: 1d9q 1dbz 1dcu
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.