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PDBsum entry 1jlh

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Isomerase PDB id
1jlh

 

 

 

 

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Contents
Protein chain
556 a.a. *
Waters ×1289
* Residue conservation analysis
PDB id:
1jlh
Name: Isomerase
Title: Human glucose-6-phosphate isomerase
Structure: Phosphoglucose isomerase. Chain: a, b, c, d. Synonym: pgi, glucose phosphate isomerase. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
Resolution:
2.10Å     R-factor:   0.197     R-free:   0.237
Authors: A.T.Cordeiro
Key ref: A.T.Cordeiro et al. (2003). Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps. Biochim Biophys Acta, 1645, 117-122. PubMed id: 12573240 DOI: 10.1016/S1570-9639(02)00464-8
Date:
16-Jul-01     Release date:   11-Feb-03    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P06744  (G6PI_HUMAN) -  Glucose-6-phosphate isomerase from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
558 a.a.
556 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.5.3.1.9  - glucose-6-phosphate isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
alpha-D-glucose 6-phosphate
= beta-D-fructose 6-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1016/S1570-9639(02)00464-8 Biochim Biophys Acta 1645:117-122 (2003)
PubMed id: 12573240  
 
 
Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps.
A.T.Cordeiro, P.H.Godoi, C.H.Silva, R.C.Garratt, G.Oliva, O.H.Thiemann.
 
  ABSTRACT  
 
The second enzyme in the glycolytic pathway, phosphoglucose isomerase (PGI), catalyses an intracellular aldose-ketose isomerization. Here we describe the human recombinant PGI structure (hPGI) solved in the absence of active site ligands. Crystals isomorphous to those previously reported were used to collect a 94% complete data set to a limiting resolution of 2.1 A. From the comparison between the free active site hPGI structure and the available human and rabbit PGI (rPGI) structures, a mechanism for protein initial catalytic steps is proposed. Binding of the phosphate moiety of the substrate to two distinct elements of the active site is responsible for driving a series of structural changes resulting in the polarisation of the active site histidine, priming it for the initial ring-opening step of catalysis.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
15716432 T.Hansen, B.Schlichting, M.Felgendreher, and P.Schönheit (2005).
Cupin-type phosphoglucose isomerases (Cupin-PGIs) constitute a novel metal-dependent PGI family representing a convergent line of PGI evolution.
  J Bacteriol, 187, 1621-1631.  
15206941 A.T.Cordeiro, P.A.Michels, L.F.Delboni, and O.H.Thiemann (2004).
The crystal structure of glucose-6-phosphate isomerase from Leishmania mexicana reveals novel active site features.
  Eur J Biochem, 271, 2765-2772.
PDB codes: 1q50 1t10
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.  
14551194 T.Hansen, D.Wendorff, and P.Schönheit (2004).
Bifunctional phosphoglucose/phosphomannose isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamily.
  J Biol Chem, 279, 2262-2272.  
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 codes are shown on the right.

 

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