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| {{Template:ColorKey_Loop}}, | | {{Template:ColorKey_Loop}}, |
| {{Template:ColorKey_Turn}}). The <scene name='47/477090/Cv/5'>active site contains a Schiff-base-bound phosphosugar</scene> at <scene name='47/477090/Cv/6'>Lys135</scene><ref>PMID:24531488</ref>. Water molecules shown as red spheres. <scene name='47/477090/Cv/7'>Cl coordination site</scene>. | | {{Template:ColorKey_Turn}}). The <scene name='47/477090/Cv/5'>active site contains a Schiff-base-bound phosphosugar</scene> at <scene name='47/477090/Cv/6'>Lys135</scene><ref>PMID:24531488</ref>. Water molecules shown as red spheres. <scene name='47/477090/Cv/7'>Cl coordination site</scene>. |
| | </StructureSection> |
| == 3D Structures of transaldolase == | | == 3D Structures of transaldolase == |
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Revision as of 22:08, 10 October 2017
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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[1].
Disease
TAL deficiency influences mitochondrial homeostasis, Ca+2 fluxing and apoptosis[2].
Structural highlights
TAL overall structure is of a TIM barrel (Alpha Helices,
Beta Strands ,
Loops ,
Turns). The active site contains a Schiff-base-bound phosphosugar at Lys135[3]. Water molecules shown as red spheres. Cl coordination site.
- ↑ Caillau M, Paul Quick W. New insights into plant transaldolase. Plant J. 2005 Jul;43(1):1-16. PMID:15960612 doi:https://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:https://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:https://dx.doi.org/10.1107/S1399004713030666
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3D Structures of transaldolase
Updated on 10-October-2017
{"openlevels":0}
- Transaldolase
- 3clm – TAL – Neisseria gonorrhoeae
- 3cwn, 1onr, 1ucw - EcTAL B – Escherichia coli
- 3kof, 1i2n, 1i2o, 1i2p, 1i2q, 1i2r, 4rz5, 4rz6 - EcTAL B (mutant)
- 3hjz – TAL B – Prochlorococcus marinus
- 3igx, 4e0c – FtTAL B – Francisella tularensis
- 3m16 – TAL – Oleispira Antarctica
- 3r8r – TAL – Bacillus subtilis
- 3r5e – TAL – Corynebacterium glutamicum
- 1f05 – TAL – human
- 1vpx – TAL – Thermotoga maritima
- 1wx0 – TAL – Thermus thermophilus
- 2cwn, 2e1d – TAL (mutant) – mouse
- Transaldolase binary complexes
- 3tk7 - FtTAL B + fructose 6-phosphate
- 3te9 - FtTAL B (mutant) + fructose 6-phosphate
- 3tkf - FtTAL B (mutant) + seduheptulose 7-phosphate
- 3tno - FtTAL B + seduheptulose 7-phosphate
- 3upb - FtTAL B + arabinose 5-phosphate
- 4s2b - EcTAL B + tagatose 6-phosphate
- 4s2c, 4s1f - EcTAL B + fructose 6-phosphate
- 4rxf, 4rxg, 4rz4 - EcTAL B (mutant) + fructose 6-phosphate
- 4xz9 - TAL + glycerol 3-phosphate – Thermoplasma acidophilum
</StructureSection>
References
