TY - JOUR
T1 - The structural organization of the PsaC protein in photosystem i from single crystal EPR and x-ray crystallographic studies
AU - Kamlowski, Andreas
AU - Van Der Est, Arthur
AU - Fromme, Petra
AU - Krauß, Norbert
AU - Schubert, Wolf Dieter
AU - Klukas, Olaf
AU - Stehlik, Dietmar
N1 - Funding Information:
We would like to thank H.-T. Witt (TU Berlin), W. Saenger (FU Berlin), C. Ross (University of Nebraska, USA), M. Piccioli (University of Florence, Italy), H. Naver (Royal Vet. and Agric. University, Copenhagen, Denmark) and C. Luchinat (University of Bologna, Italy) for helpful discussions. We also acknowledge J. Hüttermann (Universität des Saarlandes, Germany), K. Brettel (CEA Saclay, France) and H. Naver for sending us preprints. This work was supported by the Deutsche Forschungsgemeinschaft (SfB 312; Teilprojekte A1, A3 and D1).
PY - 1997/4/11
Y1 - 1997/4/11
N2 - In Photosystem I (PS I) the terminal electron accepters, F(A) and F(B), are iron-sulfur (4Fe-4S) centers, which are bound to the stromal subunit PsaC. The orientation of PsaC is determined relative to the whole PS I complex (see Schubert, W.-D. et al. (1995) in From Light to Biosphere (Mathis, P. ed.), Vol. II, pp. 3-10, Kluwer) from which a molecular model for the structure of PsaC within PS I is derived. Two strategies are followed: (i) PS I single crystal EPR data on the orientation of the g tensors of both F(A)- and F(B)- relative to each other and relative to the crystal axes (see preceding paper) are used in conjuction with the central structural part of the bacterial 2 [Fe4S4] ferredoxins, the cysteine binding motifs of which are known to be homologous to those of PsaC; (ii) the same core structure is fitted into the intermediate resolution electron density map of PS I. The PsaC orientation obtained both ways agree well. The local twofold symmetry axis inherent to the ferredoxin model leaves a twofold ambiguity in the structural conclusion. Deviations from this C2-symmetry in the amino acid sequence of PsaC are analyzed with respect to observable properties which would resolve the remaining structural ambiguity. Arguments both for and against F(A) being the distal iron-sulfur center (to F(x)) are discussed.
AB - In Photosystem I (PS I) the terminal electron accepters, F(A) and F(B), are iron-sulfur (4Fe-4S) centers, which are bound to the stromal subunit PsaC. The orientation of PsaC is determined relative to the whole PS I complex (see Schubert, W.-D. et al. (1995) in From Light to Biosphere (Mathis, P. ed.), Vol. II, pp. 3-10, Kluwer) from which a molecular model for the structure of PsaC within PS I is derived. Two strategies are followed: (i) PS I single crystal EPR data on the orientation of the g tensors of both F(A)- and F(B)- relative to each other and relative to the crystal axes (see preceding paper) are used in conjuction with the central structural part of the bacterial 2 [Fe4S4] ferredoxins, the cysteine binding motifs of which are known to be homologous to those of PsaC; (ii) the same core structure is fitted into the intermediate resolution electron density map of PS I. The PsaC orientation obtained both ways agree well. The local twofold symmetry axis inherent to the ferredoxin model leaves a twofold ambiguity in the structural conclusion. Deviations from this C2-symmetry in the amino acid sequence of PsaC are analyzed with respect to observable properties which would resolve the remaining structural ambiguity. Arguments both for and against F(A) being the distal iron-sulfur center (to F(x)) are discussed.
KW - EPR
KW - F(A)
KW - F(B)
KW - Photosystem I
KW - PsaC protein
KW - X-ray crystallography
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U2 - 10.1016/S0005-2728(96)00162-4
DO - 10.1016/S0005-2728(96)00162-4
M3 - Article
C2 - 9131044
AN - SCOPUS:0030914645
SN - 0005-2728
VL - 1319
SP - 199
EP - 213
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - 2-3
ER -