Transaldolase: Difference between revisions
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<StructureSection load='3tno' size='400' side='right' scene='47/477090/Cv/1' caption='Transaldolase dimer complex with sedoheptulose 7-phosphate and Cl- (green) ion, [[3tno]]'> | <StructureSection load='3tno' size='400' side='right' scene='47/477090/Cv/1' caption='Transaldolase dimer complex with sedoheptulose 7-phosphate and Cl- (green) ion, [[3tno]]' pspeed='8'> | ||
== Function == | == Function == | ||
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{{Template:ColorKey_Strand}}, | {{Template:ColorKey_Strand}}, | ||
{{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. | {{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>. | ||
== 3D Structures of transaldolase == | == 3D Structures of transaldolase == | ||
Revision as of 12:52, 2 April 2017
FunctionTransaldolase (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]. DiseaseTAL deficiency influences mitochondrial homeostasis, Ca+2 fluxing and apoptosis[2]. Structural highlightsTAL overall structure is of a (Alpha Helices, Beta Strands , Loops , Turns). The at [3]. Water molecules shown as red spheres. . 3D Structures of transaldolaseUpdated on 29-May-2025 {{#tree:id=OrganizedByTopic|openlevels=0|
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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