Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism-Reference-Cited by-同舟云学术

Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism

Published:2017-05-12 Issue:8 Volume:26 Page:1667-1673
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Minges Alexander¹^ORCID,Höppner Astrid²,Groth Georg¹

Affiliation:

1. Cluster of Excellence on Plant Sciences (CEPLAS), Institute of Biochemical Plant Physiology, Heinrich Heine University Düsseldorf; Düsseldorf 40204 Germany

2. X-ray Facility and Crystal Farm; Heinrich Heine University Düsseldorf; Düsseldorf 40204 Germany

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference24 articles.

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2. Regulation of pyruvate, orthophosphate dikinase by ADP-/pi-dependent reversible phosphorylation in C3 and C4 plants;Chastain;Plant Physiol Biochem,2003

3. Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion;Nakanishi;Biochemistry,2005

4. The 3.0 Å resolution crystal structure of glycosomal pyruvate phosphate dikinase from Trypanosoma brucei;Cosenza;J Mol Biol

5. Structural intermediates and directionality of the swiveling motion of pyruvate phosphate dikinase;Minges;Sci Rep,2017

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