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PDBsum entry 2pgi

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Isomerase PDB id
2pgi
Jmol
Contents
Protein chain
442 a.a. *
Waters ×184
* Residue conservation analysis
PDB id:
2pgi
Name: Isomerase
Title: The crystal structure of phosphoglucose isomerase-an enzyme autocrine motility factor activity in tumor cells
Structure: Phosphoglucose isomerase. Chain: a. Synonym: glucose-6-phosphate isomerase. Engineered: yes
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Gene: pgib. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Homo-Dimer (from PDB file)
Resolution:
2.30Å     R-factor:   0.185     R-free:   0.278
Authors: Y.-J.Sun,C.-C.Chou,W.-S.Chen,M.Meng,C.-D.Hsiao
Key ref:
Y.J.Sun et al. (1999). The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin. Proc Natl Acad Sci U S A, 96, 5412-5417. PubMed id: 10318897 DOI: 10.1073/pnas.96.10.5412
Date:
27-Oct-98     Release date:   15-Jun-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P13376  (G6PIB_GEOSE) -  Glucose-6-phosphate isomerase B
Seq:
Struc:
445 a.a.
442 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.3.1.9  - Glucose-6-phosphate isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-glucose 6-phosphate = D-fructose 6-phosphate
D-glucose 6-phosphate
= D-fructose 6-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     gluconeogenesis   2 terms 
  Biochemical function     isomerase activity     2 terms  

 

 
    Added reference    
 
 
DOI no: 10.1073/pnas.96.10.5412 Proc Natl Acad Sci U S A 96:5412-5417 (1999)
PubMed id: 10318897  
 
 
The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin.
Y.J.Sun, C.C.Chou, W.S.Chen, R.T.Wu, M.Meng, C.D.Hsiao.
 
  ABSTRACT  
 
Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3-A resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted alpha/beta structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity.
 
  Selected figure(s)  
 
Figure 6.
Fig. 6. Morphological response of rat EGF-responsive neuronal embryonic progenitor cells promoted by PGI. (A) After 4 days of cultivation in the absence of PGI, the neuronal progenitor cells formed a single sphere of undifferentiated morphology, compared with a differentiated morphology of neurite outgrowth treated with 2 ng/ml PGI (B), 20 ng/ml PGI (C), and 200 ng/ml PGI (D).
Figure 7.
Fig. 7. Electrostatic surface potential on the PGI molecule displayed with the program GRASP (63). Negative potentials (<10 kT) are colored in deep red, and positive potentials (>10 kT) are colored in deep blue. The neutral surface potential regions are depicted in white. The orientation of the molecule is the same as in Fig. 2.
 
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20628759 M.A.Troncoso-Ponce, J.Rivoal, F.J.Cejudo, S.Dorion, R.Garcés, and E.Martínez-Force (2010).
Cloning, biochemical characterisation, tissue localisation and possible post-translational regulatory mechanism of the cytosolic phosphoglucose isomerase from developing sunflower seeds.
  Planta, 232, 845-859.  
20233491 S.S.Loo, D.P.Blake, A.Mohd-Adnan, R.Mohamed, and K.L.Wan (2010).
Eimeria tenella glucose-6-phosphate isomerase: molecular characterization and assessment as a target for anti-coccidial control.
  Parasitology, 137, 1169-1177.  
19129200 C.S.Chen, C.M.Nelson, D.Khauv, S.Bennett, E.S.Radisky, Y.Hirai, M.J.Bissell, and D.C.Radisky (2009).
Homology with vesicle fusion mediator syntaxin-1a predicts determinants of epimorphin/syntaxin-2 function in mammary epithelial morphogenesis.
  J Biol Chem, 284, 6877-6884.  
19190671 D.C.Radisky, M.Stallings-Mann, Y.Hirai, and M.J.Bissell (2009).
Single proteins might have dual but related functions in intracellular and extracellular microenvironments.
  Nat Rev Mol Cell Biol, 10, 228-234.  
18692117 M.Iiizumi, W.Liu, S.K.Pai, E.Furuta, and K.Watabe (2008).
Drug development against metastasis-related genes and their pathways: a rationale for cancer therapy.
  Biochim Biophys Acta, 1786, 87.  
  19052382 Y.L.Lee, and T.T.Li (2008).
Crystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1181-1183.  
  17401215 D.Mathur, K.Anand, D.Mathur, N.Jagadish, A.Suri, and L.C.Garg (2007).
Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 353-355.  
16420469 C.Chinopoulos, and V.Adam-Vizi (2006).
Calcium, mitochondria and oxidative stress in neuronal pathology. Novel aspects of an enduring theme.
  FEBS J, 273, 433-450.  
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.  
16616498 E.P.Gianchandani, D.L.Brautigan, and J.A.Papin (2006).
Systems analyses characterize integrated functions of biochemical networks.
  Trends Biochem Sci, 31, 284-291.  
16892078 H.Pelicano, D.S.Martin, R.H.Xu, and P.Huang (2006).
Glycolysis inhibition for anticancer treatment.
  Oncogene, 25, 4633-4646.  
17074669 I.Mérida, and A.Avila-Flores (2006).
Tumor metabolism: new opportunities for cancer therapy.
  Clin Transl Oncol, 8, 711-716.  
15684571 A.Haga (2005).
[Possibility that AMF will serve as a target molecule for the diagnosis and treatment of a metastatic neoplasm]
  Yakugaku Zasshi, 125, 169-175.  
15689508 J.H.Lee, and C.J.Jeffery (2005).
The crystal structure of rabbit phosphoglucose isomerase complexed with D-sorbitol-6-phosphate, an analog of the open chain form of D-glucose-6-phosphate.
  Protein Sci, 14, 727-734.
PDB code: 1xtb
15972722 L.Wang, X.Chen, B.Tang, X.Hua, A.Klein-Szanto, and W.D.Kruger (2005).
Expression of mutant human cystathionine beta-synthase rescues neonatal lethality but not homocystinuria in a mouse model.
  Hum Mol Genet, 14, 2201-2208.  
16277685 R.Bockermann, D.Schubert, T.Kamradt, and R.Holmdahl (2005).
Induction of a B-cell-dependent chronic arthritis with glucose-6-phosphate isomerase.
  Arthritis Res Ther, 7, R1316-R1324.  
16336264 T.Hansen, B.Schlichting, J.Grötzinger, M.K.Swan, C.Davies, and P.Schönheit (2005).
Mutagenesis of catalytically important residues of cupin type phosphoglucose isomerase from Archaeoglobus fulgidus.
  FEBS J, 272, 6266-6275.  
15103138 A.T.Cordeiro, R.Hardré, P.A.Michels, L.Salmon, L.F.Delboni, and O.H.Thiemann (2004).
Leishmania mexicana mexicana glucose-6-phosphate isomerase: crystallization, molecular-replacement solution and inhibition.
  Acta Crystallogr D Biol Crystallogr, 60, 915-919.  
12595702 C.Davies, and H.Muirhead (2003).
Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function.
  Acta Crystallogr D Biol Crystallogr, 59, 453-465.
PDB code: 1n8t
12777791 C.Davies, H.Muirhead, and J.Chirgwin (2003).
The structure of human phosphoglucose isomerase complexed with a transition-state analogue.
  Acta Crystallogr D Biol Crystallogr, 59, 1111-1113.
PDB code: 1nuh
12904811 D.B.Searls (2003).
Pharmacophylogenomics: genes, evolution and drug targets.
  Nat Rev Drug Discov, 2, 613-623.  
12888295 D.C.Radisky, Y.Hirai, and M.J.Bissell (2003).
Delivering the message: epimorphin and mammary epithelial morphogenesis.
  Trends Cell Biol, 13, 426-434.  
14501126 J.Akerboom, A.P.Turnbull, D.Hargreaves, M.Fisher, D.de Geus, S.E.Sedelnikova, J.M.Berrisford, P.J.Baker, C.H.Verhees, J.van der Oost, and D.W.Rice (2003).
Purification, crystallization and preliminary crystallographic analysis of phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus.
  Acta Crystallogr D Biol Crystallogr, 59, 1822-1823.  
11983887 D.Arsenieva, R.Hardre, L.Salmon, and C.J.Jeffery (2002).
The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid.
  Proc Natl Acad Sci U S A, 99, 5872-5877.
PDB code: 1koj
11839305 L.A.Martinez-Cruz, M.K.Dreyer, D.C.Boisvert, H.Yokota, M.L.Martinez-Chantar, R.Kim, and S.H.Kim (2002).
Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A resolution infers a molecular function of 3-hexulose-6-phosphate isomerase.
  Structure, 10, 195-204.
PDB code: 1jeo
11264592 A.T.Cordeiro, P.H.Godoi, L.F.Delboni, G.Oliva, and O.H.Thiemann (2001).
Human phosphoglucose isomerase: expression, purification, crystallization and preliminary crystallographic analysis.
  Acta Crystallogr D Biol Crystallogr, 57, 592-595.  
11327814 C.J.Jeffery, R.Hardré, and L.Salmon (2001).
Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis.
  Biochemistry, 40, 1560-1566.
PDB code: 1g98
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.  
11697795 J.Zhi, D.W.Sommerfeldt, C.T.Rubin, M.Hadjiargyrou, and C.T.Rubin (2001).
Differential expression of neuroleukin in osseous tissues and its involvement in mineralization during osteoblast differentiation.
  J Bone Miner Res, 16, 1994-2004.  
11587767 M.O.Noordewier, and P.V.Warren (2001).
Gene expression microarrays and the integration of biological knowledge.
  Trends Biotechnol, 19, 412-415.  
11344151 T.Hansen, M.Oehlmann, and P.Schönheit (2001).
Novel type of glucose-6-phosphate isomerase in the hyperthermophilic archaeon Pyrococcus furiosus.
  J Bacteriol, 183, 3428-3435.  
11004567 A.Haga, Y.Niinaka, and A.Raz (2000).
Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein.
  Biochim Biophys Acta, 1480, 235-244.  
11114510 H.Erlandsen, E.E.Abola, and R.C.Stevens (2000).
Combining structural genomics and enzymology: completing the picture in metabolic pathways and enzyme active sites.
  Curr Opin Struct Biol, 10, 719-730.  
  10595547 M.Meng, T.L.Chane, Y.J.Sun, and C.D.Hsiao (1999).
Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate.
  Protein Sci, 8, 2438-2443.  
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.