Transaldolase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
{{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>.
-
'''Transaldolase''' (TAD) 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.
+
== 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]] – TAD – ''Neisseria gonorrhoeae''<br />
+
**[[3clm]] – TAL – ''Neisseria gonorrhoeae''<br />
-
**[[3cwn]], [[1onr]], [[1ucw]] - EcTAD B – ''Escherichia coli''<br />
+
**[[3cwn]], [[1onr]], [[1ucw]] - EcTAL B – ''Escherichia coli''<br />
-
**[[3kof]], [[1i2n]], [[1i2o]], [[1i2p]], [[1i2q]], [[1i2r]] - EcTAD B (mutant)<br />
+
**[[3kof]], [[1i2n]], [[1i2o]], [[1i2p]], [[1i2q]], [[1i2r]] - EcTAL B (mutant)<br />
-
**[[3hjz]] – TAD B – ''Prochlorococcus marinus''<br />
+
**[[3hjz]] – TAL B – ''Prochlorococcus marinus''<br />
-
**[[3igx]], [[4e0c]] – FtTAD B – ''Francisella tularensis''<br />
+
**[[3igx]], [[4e0c]] – FtTAL B – ''Francisella tularensis''<br />
-
**[[3m16]] – TAD – ''Oleispira Antarctica''<br />
+
**[[3m16]] – TAL – ''Oleispira Antarctica''<br />
-
**[[3r8r]] – TAD – ''Bacillus subtilis''<br />
+
**[[3r8r]] – TAL – ''Bacillus subtilis''<br />
-
**[[3r5e]] – TAD – ''Corynebacterium glutamicum''<br />
+
**[[3r5e]] – TAL – ''Corynebacterium glutamicum''<br />
-
**[[1f05]] – TAD – human<br />
+
**[[1f05]] – TAL – human<br />
-
**[[1vpx]] – TAD – ''Thermotoga maritima''<br />
+
**[[1vpx]] – TAL – ''Thermotoga maritima''<br />
-
**[[1wx0]] – TAD – ''Thermus thermophilus''<br />
+
**[[1wx0]] – TAL – ''Thermus thermophilus''<br />
-
**[[2cwn]], [[2e1d]] – TAD (mutant) – mouse<br />
+
**[[2cwn]], [[2e1d]] – TAL (mutant) – mouse<br />
*Transaldolase binary complexes
*Transaldolase binary complexes
-
**[[3tk7]] - FtTAD B + fructose 6-phosphate<br />
+
**[[3tk7]] - FtTAL B + fructose 6-phosphate<br />
-
**[[3te9]] - FtTAD B (mutant) + fructose 6-phosphate<br />
+
**[[3te9]] - FtTAL B (mutant) + fructose 6-phosphate<br />
-
**[[3tkf]] - FtTAD B (mutant) + seduheptulose 7-phosphate<br /`>
+
**[[3tkf]] - FtTAL B (mutant) + seduheptulose 7-phosphate<br /`>
-
**[[3tno]] - FtTAD B + seduheptulose 7-phosphate<br />
+
**[[3tno]] - FtTAL B + seduheptulose 7-phosphate<br />
-
**[[3upb]] - FtTAD B + arabinose 5-phosphate<br />
+
**[[3upb]] - FtTAL B + arabinose 5-phosphate<br />
}}
}}
 +
== References ==
 +
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 06:57, 19 September 2016

Template:STRUCTURE 3tno

Contents

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. The active site contains a Schiff-base-bound phosphosugar at Lys135[3].

3D Structures of transaldolase

Updated on 19-September-2016

References

  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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Retrieved from "http://52.214.119.220/wiki/index.php/Transaldolase"
Personal tools