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Literature DB >> 8989320

Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase.

Abstract

The structure of fructose 1,6-bisphosphate aldolase shows three distinct modes of product binding that are correlated to the disposition of the C-terminal region and depicts a possible trajectory for product exchange. The structure also indicates binding preference for monobasic triose phosphates.

Entities: Chemical Gene

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Year: 1997 PMID： 8989320 DOI： 10.1038/nsb0197-36

Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368

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Cited

34 in total

1. Order, disorder, and perturbations in actin-aldolase rafts.

Authors: Catherine Sukow; David J DeRosier
Journal: Biophys J Date: 2003-07 Impact factor: 4.033

2. Ion Mobility-Mass Spectrometry Reveals Highly-Compact Intermediates in the Collision Induced Dissociation of Charge-Reduced Protein Complexes.

Authors: Russell E Bornschein; Shuai Niu; Joseph Eschweiler; Brandon T Ruotolo
Journal: J Am Soc Mass Spectrom Date: 2015-09-01 Impact factor: 3.109

3. Glycolytic enzyme interactions with yeast and skeletal muscle F-actin.

Authors: Victor F Waingeh; Carol D Gustafson; Evguenii I Kozliak; Stephen L Lowe; Harvey R Knull; Kathryn A Thomasson
Journal: Biophys J Date: 2005-12-02 Impact factor: 4.033

4. Thermodynamic analysis shows conformational coupling and dynamics confer substrate specificity in fructose-1,6-bisphosphate aldolase.

Authors: John A Pezza; Jack D Stopa; Elizabeth M Brunyak; Karen N Allen; Dean R Tolan
Journal: Biochemistry Date: 2007-10-13 Impact factor: 3.162

5. Purification, crystallization and preliminary X-ray crystallographic study of the L-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8.

Authors: Jeyaraman Jeyakanthan; Junichiro Taka; Akihiro Kikuchi; Chizu Kuroishi; Katsuhide Yutani; Yoshitugu Shiro
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2005-11-24

Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase.

1. Order, disorder, and perturbations in actin-aldolase rafts.

2. Ion Mobility-Mass Spectrometry Reveals Highly-Compact Intermediates in the Collision Induced Dissociation of Charge-Reduced Protein Complexes.

3. Glycolytic enzyme interactions with yeast and skeletal muscle F-actin.

4. Thermodynamic analysis shows conformational coupling and dynamics confer substrate specificity in fructose-1,6-bisphosphate aldolase.

5. Purification, crystallization and preliminary X-ray crystallographic study of the L-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8.

6. Brownian dynamics simulations of interactions between aldolase and G- or F-actin.

7. Automated cryo-EM structure refinement using correlation-driven molecular dynamics.

8. Dramatic improvement of crystal quality for low-temperature-grown rabbit muscle aldolase.

9. Improved pKa calculations through flexibility based sampling of a water-dominated interaction scheme.

10. Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant.