| General information | | DisProt: | DP00614 | | Name: | Triosephosphate isomerase | | Synonym(s): | TPIS_PLAFA
TIM
Triose-phosphate isomerase
PfTIM
EC=5.3.1.1
| | First appeared in release: | Release 5.3 (09/21/2010) | | UniProt: | Q07412 | | UniGene: | | | SwissProt: | TPIS_PLAFA | | TrEMBL: | | | NCBI (GI): | 586112 | | Source organism: | Plasmodium falciparum | | Sequence length: | 248 | | Percent disordered: | 12% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MARKYFVAAN WKCNGTLESI KSLTNSFNNL DFDPSKLDVV VFPVSVHYDH TRKLLQSKFS - 60
TGIQNVSKFG NGSYTGEVSA EIAKDLNIEY VIIGHFERRK YFHETDEDVR EKLQASLKNN - 120
LKAVVCFGES LEQREQNKTI EVITKQVKAF VDLIDNFDNV ILAYEPLWAI GTGKTATPEQ - 180
AQLVHKEIRK IVKDTCGEKQ ANQIRILYGG SVNTENCSSL IQQEDIDGFL VGNASLKESF - 240
VDIIKSAM
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| Functional narrative |
A dimeric glycolytic enzyme, PfTIM catalyzes isomerization of D-glyeraldehyde-3-phosphate to diheydroxyacetone phosphate PfTIM also plays an important role in gluconeogenesis, the hexosemonophosphate shunt and fatty acid biosynthesis. (Velanker, 1997)
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | Loop 3 | | Location: | 66 - 80 | | Length: | 15 | | Region sequence: |
VSKFGNGSYTGEVSA | | Modification type: | Native
| | PDB: | 1YDV:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Intraprotein interaction
Protein-protein binding
| Detection methods:
- X-ray crystallography
| References:
- Espinoza-Fonseca LM, Wong-Ramirez C, Trujillo-Ferrara JG. "Tyr74 is essential for the formation, stability and function of Plasmodium falciparum triosephosphate isomerase dimer." Arch Biochem Biophys. 2010; 494(1): 46-57. PubMed: 19914198
- Velanker S S, Ray S S, Gokhale R S, Suma S, Balaram H, Balaram P, Murthy M R. "Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design." Structure (London, England : 1993). 1997; 5(6): 751-61. PubMed: 9261072
| Comments:Espinoza-Fonseca, et al., use molecular dynamic simulations to illustrate the importance of Tyr74 to the functional stability of PfTIM, especially regarding intersubunit dynamics of Loop 3.
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| Region 2 | | Type: | Disordered | | Name: | Loop 6 | | Location: | 165 - 178 | | Length: | 14 | | Region sequence: |
EPLWAIGTGKTATP | | Modification type: | Native
| | PDB: | 1YDV:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography
| References:
- Velanker S S, Ray S S, Gokhale R S, Suma S, Balaram H, Balaram P, Murthy M R. "Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design." Structure (London, England : 1993). 1997; 5(6): 751-61. PubMed: 9261072
| Comments:
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| Comments |
Sent for AV 9-20-10 (PubMed: 9261072)
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