7ASW

Crystal structure of chloroplastic thioredoxin z defines a novel type-specific target recognition

Summary for 7ASW

• Entry DOI: 10.2210/pdb7asw/pdb
• Descriptor: Thioredoxin-related protein CITRX (2 entities in total)
• Functional Keywords: ribose-5-phosphate, rossmann fold, enzyme, chloroplast, photosynthese, chlamydomonas, isomerase
• Biological source: Chlamydomonas reinhardtii
• Total number of polymer chains: 1
• Total formula weight: 16211.51

Authors

Le Moigne, T.,Gurrieri, L.,Crozet, P.,Marchand, C.H.,Zaffagnini, M.,Sparla, F.,Lemaire, S.D.,Henri, J. (deposition date: 2020-10-28, release date: 2021-05-19, Last modification date: 2024-01-31)

Primary citation

Le Moigne, T.,Gurrieri, L.,Crozet, P.,Marchand, C.H.,Zaffagnini, M.,Sparla, F.,Lemaire, S.D.,Henri, J.
Crystal structure of chloroplastic thioredoxin z defines a type-specific target recognition.
Plant J., 107:434-447, 2021

PubMed Abstract: Thioredoxins (TRXs) are ubiquitous disulfide oxidoreductases structured according to a highly conserved fold. TRXs are involved in a myriad of different processes through a common chemical mechanism. Plant TRXs evolved into seven types with diverse subcellular localization and distinct protein target selectivity. Five TRX types coexist in the chloroplast, with yet scarcely described specificities. We solved the crystal structure of a chloroplastic z-type TRX, revealing a conserved TRX fold with an original electrostatic surface potential surrounding the redox site. This recognition surface is distinct from all other known TRX types from plant and non-plant sources and is exclusively conserved in plant z-type TRXs. We show that this electronegative surface endows thioredoxin z (TRXz) with a capacity to activate the photosynthetic Calvin-Benson cycle enzyme phosphoribulokinase. The distinct electronegative surface of TRXz thereby extends the repertoire of TRX-target recognitions.

PubMed: 33930214
DOI: 10.1111/tpj.15300

Experimental method

X-RAY DIFFRACTION (2.444 Å)