PsaE is a small peripheral subunit of photosystem I (PSI) that is very accessible to the surrounding medium. It plays an essential role in optimizing the interactions with the soluble electron acceptors of PSI, ferredoxin and flavodoxin. The solution structure of PsaE from the cyanobacterium Synechocystis sp. PCC 6803 has been investigated by NMR with a special emphasis on its protein dynamic properties. PsaE is characterized by a well-defined central core that consists of a five-stranded beta-sheet (+1, +1, +1, -4x). Four loops (designated the A-B, B-C, C-D, and D-E loops) connect these beta-strands, the overall resulting structure being that of an SH3-like domain. As compared to previously determined PsaE structures, conformational differences are observed in the first three loops. The flexibility of the loops was investigated using (15)N relaxation experiments. This flexibility is small in amplitude for the A-B and B-C loops, but is large for the C-D loop, particularly in the region corresponding to the missing sequence of Nostoc sp. PCC 8009. The plasticity of the connecting loops in the free subunit is compared to that when bound to the PSI and discussed in relation to the insertion process and the function(s) of PsaE.
[NMR paper] Paramagnetic 1H NMR spectroscopy of the reduced, unbound photosystem I subunit PsaC:
Paramagnetic 1H NMR spectroscopy of the reduced, unbound photosystem I subunit PsaC: sequence-specific assignment of contact-shifted resonances and identification of mixed- and equal-valence Fe-Fe pairs in centers FA- and FB-.
Related Articles Paramagnetic 1H NMR spectroscopy of the reduced, unbound photosystem I subunit PsaC: sequence-specific assignment of contact-shifted resonances and identification of mixed- and equal-valence Fe-Fe pairs in centers FA- and FB-.
J Biol Inorg Chem. 2000 Jun;5(3):381-92
Authors: Antonkine ML, Bentrop D, Bertini I,...
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[NMR paper] Refined solution structure and backbone dynamics of 15N-labeled C12A-p8MTCP1 studied
Refined solution structure and backbone dynamics of 15N-labeled C12A-p8MTCP1 studied by NMR relaxation.
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J Biomol NMR. 1999 Dec;15(4):271-88
Authors: Barthe P, Chiche L, Declerck N, Delsuc MA, Lefèvre JF, Malliavin T, Mispelter J, Stern MH, Lhoste JM, Roumestand C
MTCP1 (for Mature-T-Cell Proliferation) was the first gene unequivocally identified in the group of uncommon leukemias with a mature phenotype. The...
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[NMR paper] Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) f
Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site.
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Biochemistry. 1998 Aug 4;37(31):10881-96
Authors: Feng W, Tejero R, Zimmerman DE, Inouye M, Montelione GT
The major cold-shock protein (CspA) from Escherichia...
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Solution NMR structure of photosystem II reaction center protein Psb28 from Synechocy
Solution NMR structure of photosystem II reaction center protein Psb28 from Synechocystis sp. Strain PCC 6803.
Solution NMR structure of photosystem II reaction center protein Psb28 from Synechocystis sp. Strain PCC 6803.
Proteins. 2010 Sep 22;
Authors: Yang Y, Ramelot TA, Cort JR, Wang D, Ciccosanti C, Hamilton K, Nair R, Rost B, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
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[NMR paper] Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhi
Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.
Biochemistry. 1996 Feb 6;35(5):1516-24
Authors: Liu J, Prakash O, Cai M, Gong Y, Huang Y, Wen L, Wen JJ, Huang JK, Krishnamoorthi R
The solution structure of recombinant Cucurbita maxima trypsin...
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[NMR paper] 1H and 15N NMR assignments of PsaE, a photosystem I subunit from the cyanobacterium S
1H and 15N NMR assignments of PsaE, a photosystem I subunit from the cyanobacterium Synechococcus sp. strain PCC 7002.
Related Articles 1H and 15N NMR assignments of PsaE, a photosystem I subunit from the cyanobacterium Synechococcus sp. strain PCC 7002.
Biochemistry. 1994 May 24;33(20):6043-51
Authors: Falzone CJ, Kao YH, Zhao J, MacLaughlin KL, Bryant DA, Lecomte JT
PsaE is a highly conserved, water-soluble protein of the photosystem I reaction center complexes of cyanobacteria, algae, and green plants. Along with the PsaC and PsaD proteins,...
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[NMR paper] 1H and 15N NMR assignments of PsaE, a photosystem I subunit from the cyanobacterium S
1H and 15N NMR assignments of PsaE, a photosystem I subunit from the cyanobacterium Synechococcus sp. strain PCC 7002.
Related Articles 1H and 15N NMR assignments of PsaE, a photosystem I subunit from the cyanobacterium Synechococcus sp. strain PCC 7002.
Biochemistry. 1994 May 24;33(20):6043-51
Authors: Falzone CJ, Kao YH, Zhao J, MacLaughlin KL, Bryant DA, Lecomte JT
PsaE is a highly conserved, water-soluble protein of the photosystem I reaction center complexes of cyanobacteria, algae, and green plants. Along with the PsaC and PsaD proteins,...
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[NMR paper] Investigation of the local structure and dynamics of the H subunit of the mitochondri
Investigation of the local structure and dynamics of the H subunit of the mitochondrial glycine decarboxylase using heteronuclear NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Investigation of the local structure and dynamics of the H subunit of the mitochondrial glycine decarboxylase using heteronuclear NMR spectroscopy.
Biochemistry. 1999 Jun 29;38(26):8334-46
Authors: Guilhaudis L, Simorre JP, Blackledge M, Neuburger M, Bourguignon J, Douce R, Marion D, Gans P
The...
Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I fro
Linear Mode
