2VYQ

FERREDOXIN:NADP REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR, LEU 263 REPLACED BY PRO AND TYR 303 REPLACED BY SER (T155G-A160T-L263P-Y303S)

Summary for 2VYQ

• Entry DOI: 10.2210/pdb2vyq/pdb
• Related: 1B2R 1BJK 1BQE 1E62 1E63 1E64 1EWY 1GJR 1GO2 1GR1 1H42 1H85 1OGI 1OGJ 1QGY 1QGZ 1QH0 1QUE 1QUF 1W34 1W35 1W87 2BMW 2BSA 2VZL
• Descriptor: FERREDOXIN-NADP REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (5 entities in total)
• Functional Keywords: phycobilisome, oxidoreductase, fad, nadp, membrane, thylakoid, flavoprotein
• Biological source: NOSTOC SP.
• Cellular location: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side: P21890
• Total number of polymer chains: 1
• Total formula weight: 35133.49

Authors

Herguedas, B.,Martinez-Julvez, M.,Hermoso, J.A.,Peregrina, J.R.,Medina, M. (deposition date: 2008-07-28, release date: 2009-04-21, Last modification date: 2023-12-13)

Primary citation

Peregrina, J.R.,Herguedas, B.,Hermoso, J.A.,Martinez-Julvez, M.,Medina, M.
Protein Motifs Involved in Coenzyme Interaction and Enzymatic Efficiency in Anabaena Ferredoxin-Nadp+ Reductase.
Biochemistry, 48:3109-, 2009

PubMed Abstract: Ferredoxin-NADP+ reductases (FNRs) must determine the coenzyme specificity and allow the transient encounter between N5 of its flavin cofactor and C4 of the coenzyme nicotinamide for efficient hydride transfer. Combined site-directed replacements in different putative determinants of the FNR coenzyme specificity were simultaneously produced. The resulting variants were structurally and functionally analyzed for their binding and hydride transfer abilities to the FNR physiological coenzyme NADP+/H, as well as to NAD+/H. The previously studied Y303S mutation is the only one that significantly enhances specificity for NAD+. Combination of mutations from the pyrophosphate or 2'-phosphate regions, even including Y303S, does not improve activity with NAD+, despite structures of these FNRs show how particular coenzyme-binding regions resembled motifs found in NAD+/H-dependent enzymes of the FNR family. Therefore, the "rational approach" did not succeed well, and coenzyme specificity redesign in the FNR family will be more complex than that anticipated in other NADP+/NAD+ families.

PubMed: 19219975
DOI: 10.1021/BI802077C

Experimental method

X-RAY DIFFRACTION (1.9 Å)