Structure of the Mg-chelatase cofactor GUN4 reveals a novel hand-shaped fold for porphyrin binding.
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Structural Insights into the Catalytic Mechanism of Synechocystis Magnesium Protoporphyrin IX O -Methyltransferase (ChlM)Crystal structure of the catalytic subunit of magnesium chelataseTetrapyrrole Signaling in PlantsVASCo: computation and visualization of annotated protein surface contacts.Porphyrin Binding to Gun4 Protein, Facilitated by a Flexible Loop, Controls Metabolite Flow through the Chlorophyll Biosynthetic Pathway.Chloroplast evolution, structure and functions.Comparative analysis of the Spirulina platensis subcellular proteome in response to low- and high-temperature stresses: uncovering cross-talk of signaling components.Arabidopsis miR171-targeted scarecrow-like proteins bind to GT cis-elements and mediate gibberellin-regulated chlorophyll biosynthesis under light conditions.Tetrapyrrole Metabolism in Arabidopsis thaliana.A synthetic de-greening gene circuit provides a reporting system that is remotely detectable and has a re-set capacity.GUN4-Protoporphyrin IX Is a Singlet Oxygen Generator with Consequences for Plastid Retrograde Signaling.The steady-state level of Mg-protoporphyrin IX is not a determinant of plastid-to-nucleus signaling in Arabidopsis.Tetrapyrrole-based drought stress signalling.Porphyrins promote the association of GENOMES UNCOUPLED 4 and a Mg-chelatase subunit with chloroplast membranes.Organization of chlorophyll biosynthesis and insertion of chlorophyll into the chlorophyll-binding proteins in chloroplasts.Importance of the cyanobacterial Gun4 protein for chlorophyll metabolism and assembly of photosynthetic complexes.Structure of GUN4 from Chlamydomonas reinhardtii.Structure of the cyanobacterial Magnesium Chelatase H subunit determined by single particle reconstruction and small-angle X-ray scattering.Structural and functional consequences of removing the N-terminal domain from the magnesium chelatase ChlH subunit of Thermosynechococcus elongatus.Identification and molecular characterization of the second Chlamydomonas gun4 mutant, gun4-II.BchJ and BchM interact in a 1 : 1 ratio with the magnesium chelatase BchH subunit of Rhodobacter capsulatus.Characterization of the magnesium chelatase from Thermosynechococcus elongatus.Kinetic analyses of the magnesium chelatase provide insights into the mechanism, structure, and formation of the complex.The Mg-chelatase H subunit is an abscisic acid receptor.Phosphorylation of GENOMES UNCOUPLED 4 Alters Stimulation of Mg Chelatase Activity in Angiosperms.
P2860
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P2860
Structure of the Mg-chelatase cofactor GUN4 reveals a novel hand-shaped fold for porphyrin binding.
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2005 nî lūn-bûn
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2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
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2005年論文
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2005年論文
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2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
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name
Structure of the Mg-chelatase ...... ped fold for porphyrin binding
@nl
Structure of the Mg-chelatase ...... ed fold for porphyrin binding.
@ast
Structure of the Mg-chelatase ...... ed fold for porphyrin binding.
@en
type
label
Structure of the Mg-chelatase ...... ped fold for porphyrin binding
@nl
Structure of the Mg-chelatase ...... ed fold for porphyrin binding.
@ast
Structure of the Mg-chelatase ...... ed fold for porphyrin binding.
@en
prefLabel
Structure of the Mg-chelatase ...... ped fold for porphyrin binding
@nl
Structure of the Mg-chelatase ...... ed fold for porphyrin binding.
@ast
Structure of the Mg-chelatase ...... ed fold for porphyrin binding.
@en
P2093
P2860
P3181
P1433
P1476
Structure of the Mg-chelatase ...... ed fold for porphyrin binding.
@en
P2093
Jean-Luc Ferrer
Joseph P Noel
Mark A Verdecia
Robert M Larkin
Roland Riek
P2860
P3181
P356
10.1371/JOURNAL.PBIO.0030151
P407
P577
2005-04-26T00:00:00Z