ArticlePhotosynthesis research2003
Amino acid sequences and solution structures of manganese stabilizing protein that affect reconstitution of Photosystem II activity.
Article in Photosynthesis research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- An intrinsically disordered photosystem II subunit, PsbO, provides a structural template and a sensor of the hydrogen-bonding network in photosynthetic water oxidation.The Journal of biological chemistry · 2013Article
- Article
- Probing the topography of the photosystem II oxygen evolving complex: PsbO is required for efficient calcium protection of the manganese cluster against dark-inhibition by an artificial reductant.Photosynthesis research · 2011Article
- The importance of protein-protein interactions for optimising oxygen activity in photosystem II: reconstitution with a recombinant thioredoxin--manganese stabilising protein.Photosynthesis research · 2007Article
- Structure and activity of the photosystem II manganese-stabilizing protein: role of the conserved disulfide bond.Photosynthesis research · 2005Article
- Soybean genotypic difference in growth, nutrient accumulation and ultrastructure in response to manganese and iron supply in solution culture.Annals of botany · 2005Article
- Assembly and function of the photosystem II manganese stabilizing protein: lessons from its natively unfolded behavior.Photosynthesis research · 2005Article
- Analysis of the Structure of the PsbO Protein and its Implications.Photosynthesis research · 2004Article
- Structural and functional aspects of the MSP (PsbO) and study of its differences in thermophilic versus mesophilic organisms.Photosynthesis researchReview
- Structures and functions of the extrinsic proteins of photosystem II from different species.Photosynthesis researchReview
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This minireview presents a summary of information available on the secondary and tertiary structure of manganese stabilizing protein (MSP) in solution, and on the identity of amino acid residues that affect binding and functional assembly of this protein into Photosystem II. New data on the secondary structure of C-terminal mutants and 90 degrees C-heated manganese stabilizing protein, along with earlier data on the secondary structure of N-terminal mutants and the tertiary structure of all modified MSP species, allow for an evaluation of models for spinach MSP secondary and tertiary structure. This summary of previous and new information better documents the natively unfolded behavior of the protein in solution. A two-step mechanism for binding of manganese stabilizing protein to Photosystem II is discussed and possible solution three-dimensional conformations of the wild-type protein and some of its unfolded mutants, are proposed.
Identifiers
16228381What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.