期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 66, 期 7, 页码 1257-1270出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-009-8673-x
关键词
PsaC; Photosystem I; C-2-symmetry; PsaD; stromal proteins; reaction center; iron-sulfur cluster
资金
- National Science Foundation [MCB-0519743]
- United States Department of Energy [DE-FG-02-98-ER20314]
The elucidation of assembly pathways of multi-subunit membrane proteins is of growing interest in structural biology. In this study, we provide an analysis of the assembly of the asymmetrically oriented PsaC subunit on the pseudo C-2-symmetric Photosystem I core. Based on a comparison of the differences in the NMR solution structure of unbound PsaC with that of the X-ray crystal structure of bound PsaC, and on a detailed analysis of the PsaC binding site surrounding the F-X iron-sulfur cluster, two models can be envisioned for what are likely the last steps in the assembly of Photosystem I. Here, we dissect both models and attempt to address heretofore unrecognized issues by proposing a mechanism that includes a thermodynamic perspective. Experimental strategies to verify the models are proposed. In closing, the evolutionary aspects of the assembly process will be considered, with special reference to the structural arrangement of the PsaC binding surface.
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