Transaldolase: Difference between revisions
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{{STRUCTURE_3tno| PDB=3tno | SIZE=400| SCENE= |right|CAPTION=Transaldolase dimer complex with sedoheptulose 7-phosphate and Cl- (green) ion, [[3tno]] }} | {{STRUCTURE_3tno| PDB=3tno | SIZE=400| SCENE= |right|CAPTION=Transaldolase dimer complex with sedoheptulose 7-phosphate and Cl- (green) ion, [[3tno]] }} | ||
== Function == | |||
'''Transaldolase''' (TAL) is part of the pentose phosphate pathway. It catalyzes the transformation of sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate to erythrose 4-phosphate and fructose 6-phosphate<ref>PMID:15960612</ref>. | |||
== Disease == | |||
TAL deficiency influences mitochondrial homeostasis, Ca+2 fluxing and apoptosis<ref>PMID:18498245</ref>. | |||
== Structural highlights == | |||
TAL overall structure is of a TIM barrel. The active site contains a Schiff-base-bound phosphosugar at Lys135<ref>PMID:24531488</ref>. | |||
== 3D Structures of transaldolase == | == 3D Structures of transaldolase == | ||
| Line 10: | Line 15: | ||
*Transaldolase | *Transaldolase | ||
**[[3clm]] – | **[[3clm]] – TAL – ''Neisseria gonorrhoeae''<br /> | ||
**[[3cwn]], [[1onr]], [[1ucw]] - | **[[3cwn]], [[1onr]], [[1ucw]] - EcTAL B – ''Escherichia coli''<br /> | ||
**[[3kof]], [[1i2n]], [[1i2o]], [[1i2p]], [[1i2q]], [[1i2r]] - | **[[3kof]], [[1i2n]], [[1i2o]], [[1i2p]], [[1i2q]], [[1i2r]] - EcTAL B (mutant)<br /> | ||
**[[3hjz]] – | **[[3hjz]] – TAL B – ''Prochlorococcus marinus''<br /> | ||
**[[3igx]], [[4e0c]] – | **[[3igx]], [[4e0c]] – FtTAL B – ''Francisella tularensis''<br /> | ||
**[[3m16]] – | **[[3m16]] – TAL – ''Oleispira Antarctica''<br /> | ||
**[[3r8r]] – | **[[3r8r]] – TAL – ''Bacillus subtilis''<br /> | ||
**[[3r5e]] – | **[[3r5e]] – TAL – ''Corynebacterium glutamicum''<br /> | ||
**[[1f05]] – | **[[1f05]] – TAL – human<br /> | ||
**[[1vpx]] – | **[[1vpx]] – TAL – ''Thermotoga maritima''<br /> | ||
**[[1wx0]] – | **[[1wx0]] – TAL – ''Thermus thermophilus''<br /> | ||
**[[2cwn]], [[2e1d]] – | **[[2cwn]], [[2e1d]] – TAL (mutant) – mouse<br /> | ||
*Transaldolase binary complexes | *Transaldolase binary complexes | ||
**[[3tk7]] - | **[[3tk7]] - FtTAL B + fructose 6-phosphate<br /> | ||
**[[3te9]] - | **[[3te9]] - FtTAL B (mutant) + fructose 6-phosphate<br /> | ||
**[[3tkf]] - | **[[3tkf]] - FtTAL B (mutant) + seduheptulose 7-phosphate<br /`> | ||
**[[3tno]] - | **[[3tno]] - FtTAL B + seduheptulose 7-phosphate<br /> | ||
**[[3upb]] - | **[[3upb]] - FtTAL B + arabinose 5-phosphate<br /> | ||
}} | }} | ||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:57, 19 September 2016
FunctionFunction
Transaldolase (TAL) is part of the pentose phosphate pathway. It catalyzes the transformation of sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate to erythrose 4-phosphate and fructose 6-phosphate[1].
DiseaseDisease
TAL deficiency influences mitochondrial homeostasis, Ca+2 fluxing and apoptosis[2].
Structural highlightsStructural highlights
TAL overall structure is of a TIM barrel. The active site contains a Schiff-base-bound phosphosugar at Lys135[3].
3D Structures of transaldolase3D Structures of transaldolase
Updated on 19-September-2016
ReferencesReferences
- ↑ Caillau M, Paul Quick W. New insights into plant transaldolase. Plant J. 2005 Jul;43(1):1-16. PMID:15960612 doi:http://dx.doi.org/TPJ2427
- ↑ Qian Y, Banerjee S, Grossman CE, Amidon W, Nagy G, Barcza M, Niland B, Karp DR, Middleton FA, Banki K, Perl A. Transaldolase deficiency influences the pentose phosphate pathway, mitochondrial homoeostasis and apoptosis signal processing. Biochem J. 2008 Oct 1;415(1):123-34. doi: 10.1042/BJ20080722. PMID:18498245 doi:http://dx.doi.org/10.1042/BJ20080722
- ↑ Light SH, Minasov G, Duban ME, Anderson WF. Adherence to Burgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):544-52. doi:, 10.1107/S1399004713030666. Epub 2014 Jan 31. PMID:24531488 doi:http://dx.doi.org/10.1107/S1399004713030666