Transaldolase: Difference between revisions

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{{STRUCTURE_3tno| PDB=3tno  | SIZE=350| SCENE= |right|CAPTION=Transaldolase dimer complex with sedoheptulose 7-phosphate and Cl- (green) ion, [[3tno]] }}
<StructureSection load='' size='400' side='right' scene='47/477090/Cv/1' caption='Transaldolase dimer complex with sedoheptulose 7-phosphate and Cl- (green) ion, [[3tno]]' pspeed='8'>
__TOC__
== Function ==
== 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>.
'''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>.
See also [[Calvin cycle]] and [[Lysine-cysteine NOS bonds]].


== Disease ==
== Disease ==
Line 7: Line 9:


== Structural highlights ==
== 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>.
TAL overall structure is of a <scene name='47/477090/Cv/8'>TIM barrel</scene> ({{Template:ColorKey_Helix}},
{{Template:ColorKey_Strand}},
{{Template:ColorKey_Loop}},
{{Template:ColorKey_Turn}}). The <scene name='47/477090/Cv/9'>active site contains a Schiff-base-bound phosphosugar</scene> at <scene name='47/477090/Cv/10'>Lys135</scene><ref>PMID:24531488</ref>. Water molecules are shown as red spheres. <scene name='47/477090/Cv/11'>Cl coordination site</scene>.
== 3D Structures of transaldolase ==
== 3D Structures of transaldolase ==
[[Transaldolase 3D structures]]
</StructureSection>


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Transaldolase
**[[3clm]] – TAL – ''Neisseria gonorrhoeae''<br />
**[[3cwn]],  [[1onr]], [[1ucw]] - EcTAL B – ''Escherichia coli''<br />
**[[3kof]], [[1i2n]], [[1i2o]], [[1i2p]], [[1i2q]], [[1i2r]], [[4rz5]], [[4rz6]] - EcTAL B (mutant)<br />
**[[3hjz]] – TAL B – ''Prochlorococcus marinus''<br />
**[[3igx]], [[4e0c]] – FtTAL B – ''Francisella tularensis''<br />
**[[3m16]] – TAL – ''Oleispira Antarctica''<br />
**[[3r8r]] – TAL – ''Bacillus subtilis''<br />
**[[3r5e]] – TAL – ''Corynebacterium glutamicum''<br />
**[[1f05]] – TAL – human<br />
**[[1vpx]] – TAL – ''Thermotoga maritima''<br />
**[[1wx0]] – TAL – ''Thermus thermophilus''<br />
**[[2cwn]], [[2e1d]] – TAL (mutant) – mouse<br />
*Transaldolase binary complexes
**[[3tk7]] - FtTAL B + fructose 6-phosphate<br />
**[[3te9]] - FtTAL B (mutant) + fructose 6-phosphate<br />
**[[3tkf]] - FtTAL B (mutant) + seduheptulose 7-phosphate<br /`>
**[[3tno]] - FtTAL B + seduheptulose 7-phosphate<br />
**[[3upb]] - FtTAL B + arabinose 5-phosphate<br />
**[[4s2b]] - EcTAL B + tagatose 6-phosphate<br />
**[[4s2c]], [[4s1f]] - EcTAL B + fructose 6-phosphate<br />
**[[4rxf]], [[4rxg]], [[4rz4]] - EcTAL B (mutant) + fructose 6-phosphate<br />
**[[4xz9]] - TAL + glycerol 3-phosphate – ''Thermoplasma acidophilum''<br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 16:55, 4 January 2023

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].

See also Calvin cycle and Lysine-cysteine NOS bonds.

Disease

TAL deficiency influences mitochondrial homeostasis, Ca+2 fluxing and apoptosis[2].

Structural highlights

TAL overall structure is of a (Alpha Helices,

 Beta Strands ,  Loops , Turns). The at [3]. Water molecules are shown as red spheres. .

3D Structures of transaldolase

Transaldolase 3D structures

Transaldolase dimer complex with sedoheptulose 7-phosphate and Cl- (green) ion, 3tno

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

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Michal Harel, Alexander Berchansky, Joel L. Sussman
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