1k0t: Difference between revisions

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New page: left|200px<br /><applet load="1k0t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k0t" /> '''NMR SOLUTION STRUCTURE OF UNBOUND, OXIDIZED ...
 
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[[Image:1k0t.gif|left|200px]]<br /><applet load="1k0t" size="450" color="white" frame="true" align="right" spinBox="true"
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'''NMR SOLUTION STRUCTURE OF UNBOUND, OXIDIZED PHOTOSYSTEM I SUBUNIT PSAC, CONTAINING [4FE-4S] CLUSTERS FA AND FB'''<br />


==Overview==
==NMR SOLUTION STRUCTURE OF UNBOUND, OXIDIZED PHOTOSYSTEM I SUBUNIT PSAC, CONTAINING [4FE-4S] CLUSTERS FA AND FB==
This work presents the three-dimensional NMR solution structure of, recombinant, oxidized, unbound PsaC from Synechococcus sp. PCC 7002., Constraints are derived from homo- and heteronuclear one-, two- and, three-dimensional (1)H and (15)N NMR data. Significant differences are, outlined between the unbound PsaC structure presented here and the, available X-ray structure of bound PsaC as an integral part of the whole, cyanobacterial PS I complex. These differences mainly concern the, arrangement of the N- and C-termini with respect to the [4Fe-4S] core, domain. In the NMR solution structure of PsaC the C-terminal region, assumes a disordered helical conformation, and is clearly different from, the extended coil conformation, which is one of the structural elements, required to anchor PsaC to the PS I core heterodimer. In solution the, N-terminus of PsaC is in contact with the pre-C-terminal region but slides, in between the latter and the iron-sulfur core region of the protein., Together, these features result in a concerted movement of the N-terminus, and pre-C-terminal region away from the F(A) binding site, accompanied by, a bending of the N-terminus. In comparison, the same terminal regions are, positioned much closer to F(A) and take up an anti-parallel beta-sheet, arrangement in PsaC bound to PS I. The conformational changes between, bound and unbound PsaC correlate with the differences reported earlier for, the EPR spectra of reduced F(A) and F(B) in bound versus unbound PsaC. The, observed different structural features in solution are highly relevant for, unraveling the stepwise assembly process of the stromal PsaC, PsaD and, PsaE subunits to the PS I core heterodimer. Electronic supplementary, material to this paper can be obtained by using the Springer Link server, located at http://dx.doi.org/10.1007/s00775-001-0321-3.
<StructureSection load='1k0t' size='340' side='right'caption='[[1k0t]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1k0t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._PCC_7002 Synechococcus sp. PCC 7002]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K0T FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k0t OCA], [https://pdbe.org/1k0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k0t RCSB], [https://www.ebi.ac.uk/pdbsum/1k0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k0t ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PSAC_SYNP2 PSAC_SYNP2] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.[HAMAP-Rule:MF_01303]  Mutant proteins with a 3Fe-4S center are not observed bound to PSI in vitro, and are probably not able to do so in vivo.[HAMAP-Rule:MF_01303]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/1k0t_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k0t ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1K0T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.] with SF4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K0T OCA].
*[[Photosystem I 3D structures|Photosystem I 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Solution structure of the unbound, oxidized Photosystem I subunit PsaC, containing [4Fe-4S] clusters F(A) and F(B): a conformational change occurs upon binding to photosystem I., Antonkine ML, Liu G, Bentrop D, Bryant DA, Bertini I, Luchinat C, Golbeck JH, Stehlik D, J Biol Inorg Chem. 2002 Apr;7(4-5):461-72. Epub 2002 Jan 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11941504 11941504]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Synechococcus sp. PCC 7002]]
[[Category: Synechococcus sp.]]
[[Category: Antonkine ML]]
[[Category: Antonkine, M.L.]]
[[Category: Bentrop D]]
[[Category: Bentrop, D.]]
[[Category: Bertini I]]
[[Category: Bertini, I.]]
[[Category: Bryant DA]]
[[Category: Bryant, D.A.]]
[[Category: Golbeck JH]]
[[Category: Golbeck, J.H.]]
[[Category: Liu G]]
[[Category: Liu, G.]]
[[Category: Luchinat C]]
[[Category: Luchinat, C.]]
[[Category: Stehlik D]]
[[Category: Stehlik, D.]]
[[Category: SF4]]
[[Category: conformational change]]
[[Category: electron transport]]
[[Category: iron-sulfur protein]]
[[Category: nmr]]
[[Category: paramagnetic]]
[[Category: photosystem i]]
[[Category: psac]]
[[Category: solution structure]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:45:42 2007''

Latest revision as of 10:56, 3 April 2024

NMR SOLUTION STRUCTURE OF UNBOUND, OXIDIZED PHOTOSYSTEM I SUBUNIT PSAC, CONTAINING [4FE-4S] CLUSTERS FA AND FBNMR SOLUTION STRUCTURE OF UNBOUND, OXIDIZED PHOTOSYSTEM I SUBUNIT PSAC, CONTAINING [4FE-4S] CLUSTERS FA AND FB

Structural highlights

1k0t is a 1 chain structure with sequence from Synechococcus sp. PCC 7002. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PSAC_SYNP2 Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.[HAMAP-Rule:MF_01303] Mutant proteins with a 3Fe-4S center are not observed bound to PSI in vitro, and are probably not able to do so in vivo.[HAMAP-Rule:MF_01303]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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