scholarly journals Overexpression of the triose phosphate translocator (TPT) complements the abnormal metabolism and development of plastidial glycolytic glyceraldehyde-3-phosphate dehydrogenase mutants

2017 ◽  
Vol 89 (6) ◽  
pp. 1146-1158 ◽  
Author(s):  
María Flores-Tornero ◽  
Armand D. Anoman ◽  
Sara Rosa-Téllez ◽  
Walid Toujani ◽  
Andreas P.M. Weber ◽  
...  
Keyword(s):  
Triose Phosphate ◽  
Phosphate Translocator ◽  
Abnormal Metabolism

scholarly journals Free energy landscape for the entire transport cycle of triose-phosphate/phosphate translocator

2017 ◽  
Author(s):  
Mizuki Takemoto ◽  
Yongchan Lee ◽  
Ryuichiro Ishitani ◽  
Osamu Nureki
Keyword(s):  
Free Energy ◽  
Conformational Changes ◽  
Conformational Transition ◽  
Substrate Binding ◽  
Energy Landscape ◽  
Umbrella Sampling ◽  
Free Energy Landscape ◽  
Coupling Mechanism ◽  
Triose Phosphate ◽  
Phosphate Translocator

AbstractSecondary active transporters translocate their substrates using the electrochemical potentials of other chemicals, undergoing large-scale conformational changes. Despite extensive structural studies, the atomic details of the transport mechanism still remain elusive. Here we performed a series of all-atom molecular dynamics simulations of the triose-phosphate/phosphate translocator (TPT), which exports organic phosphates in the chloroplast stroma in strict counter exchange with inorganic phosphate (Pi). Biased sampling methods, including string method and umbrella sampling, successfully reproduced the conformational changes between the inward– and outward-facing states, along with the substrate binding. The free energy landscape of this entire TPT transition pathway demonstrated the alternating access and substrate translocation mechanisms, which revealed Pi is relayed by positively charged residues along the transition pathway. Furthermore, the conserved Glu207 functions as a “molecular switch”, linking the local substrate binding and the global conformational transition. Our results provide atomic-detailed insights into the energy coupling mechanism of antiporter.

Molecular cloning and expression analysis of the rice triose phosphate/phosphate translocator gene

Plant Science ◽  
2002 ◽  
Vol 162 (5) ◽  
pp. 785-790 ◽  
Author(s):  
Qingmei Wang ◽  
Jia Chen ◽  
Xuechen Wang ◽  
Jinyue Sun ◽  
Wei Sha
Keyword(s):  
Molecular Cloning ◽  
Expression Analysis ◽  
Cloning And Expression ◽  
Triose Phosphate ◽  
Phosphate Translocator

scholarly journals Structure of the triose-phosphate/phosphate translocator reveals the basis of substrate specificity

Nature Plants ◽  
2017 ◽  
Vol 3 (10) ◽  
pp. 825-832 ◽  
Author(s):  
Yongchan Lee ◽  
Tomohiro Nishizawa ◽  
Mizuki Takemoto ◽  
Kaoru Kumazaki ◽  
Keitaro Yamashita ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Triose Phosphate ◽  
Phosphate Translocator

scholarly journals Analysis of a Triose Phosphate/Phosphate Translocator-Deficient Mutant Reveals a Limited Capacity for Starch Synthesis in Rice Leaves

2014 ◽  
Vol 7 (11) ◽  
pp. 1705-1708 ◽  
Author(s):  
Sang-Kyu Lee ◽  
Joon-Seob Eom ◽  
Lars M. Voll ◽  
Christian M. Prasch ◽  
Youn-Il Park ◽  
...  
Keyword(s):  
Starch Synthesis ◽  
Limited Capacity ◽  
Deficient Mutant ◽  
Triose Phosphate ◽  
Phosphate Translocator ◽  
Rice Leaves

scholarly journals Free Energy Landscape for the Entire Transport Cycle of Triose-Phosphate/Phosphate Translocator

Structure ◽  
2018 ◽  
Vol 26 (9) ◽  
pp. 1284-1296.e4 ◽  
Author(s):  
Mizuki Takemoto ◽  
Yongchan Lee ◽  
Ryuichiro Ishitani ◽  
Osamu Nureki
Keyword(s):  
Free Energy ◽  
Energy Landscape ◽  
Free Energy Landscape ◽  
Triose Phosphate ◽  
Phosphate Translocator ◽  
Transport Cycle

scholarly journals Structure of the triose-phosphate/phosphate translocator reveals the basis of substrate specificity

2017 ◽  
Author(s):  
Yongchan Lee ◽  
Tomohiro Nishizawa ◽  
Mizuki Takemoto ◽  
Kaoru Kumazaki ◽  
Keitaro Yamashita ◽  
...  
Keyword(s):  
Inorganic Phosphate ◽  
Structural Information ◽  
Chloroplast Envelope ◽  
Triose Phosphate ◽  
Phosphate Translocator ◽  
Drug Metabolite ◽  
Tightly Coupled ◽  
Group A ◽  
Dynamics Simulations ◽  
Metabolite Transporter

AbstractThe triose-phosphate/phosphate translocator (TPT) catalyzes the strict 1:1 exchange of triose phosphate, 3-phosphoglycerate and inorganic phosphate across the chloroplast envelope, and plays crucial roles in photosynthesis. Despite rigorous studies for more than 40 years, the molecular mechanism of TPT is poorly understood due to the lack of structural information. Here we report crystal structures of TPT bound to two different substrates, 3-phosphoglycerate and inorganic phosphate, in occluded conformations. The structures reveal that TPT adopts a 10-transmembrane drug/metabolite transporter fold. Both substrates are bound within the same central pocket, where conserved lysine, arginine, and tyrosine residues recognize the shared phosphate group. A structural comparison with the outward-open conformation of the bacterial drug/metabolite transporter suggests a rocking-type motion of helix bundles, and molecular dynamics simulations support a model in which this helix rocking is tightly coupled to the substrate binding, to ensure strict 1:1 exchange. These results reveal the unique mechanism of sugar phosphate/phosphate exchange by TPT.

Structure and Function of the Chloroplast Triose Phosphate — Phosphate Translocator

1992 ◽  
pp. 667-674 ◽  
Author(s):  
Ulf-Ingo Flügge ◽  
Andreas Weber ◽  
Karsten Fischer ◽  
Brigitte Loddenkötter ◽  
Holger Wallmeier
Keyword(s):  
Structure And Function ◽  
Triose Phosphate ◽  
Phosphate Translocator ◽  
And Function
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