1k0t

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 Agmenellum quadruplicatum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Gene: psac (Agmenellum quadruplicatum) 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. Publication Abstract from PubMed 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. 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:11941504 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Photosystem I

spinqualitylabelsall models 1k0t, 30 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image