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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Jackson, Simon A. Hinds, Mark G. Eaton-rye, Julian J. |
| Description | Author Affiliation: Jackson SA ( Department of Biochemistry, University of Otago, Dunedin, New Zealand.) |
| Abstract | The structure of the CyanoP subunit of photosystem II from the cyanobacterium Synechocystis sp. PCC 6803 has been determined in solution by Nuclear Magnetic Resonance spectroscopy. Combined with homology modeling of PsbP-like structures we have identified distinct structural differences between PsbP homologues which may account for the functional differences apparent between members of this protein family. A surface cleft containing a large number of conserved residues found only in CyanoP and PsbP-like homologues has been identified and our findings suggest that one of the potential cation binding sites found in CyanoP may be functionally significant. Evidence for the evolution and divergence of the PsbP super family is presented from a structural perspective including identification of residues which distinguish the PsbP family from unrelated proteins with a similar domain fold. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: from Natural to Artificial. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 8 |
| Volume Number | 1817 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2012-08-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Chemistry Photosystem II Protein Complex Synechocystis Amino Acid Sequence Binding Sites Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Protein Structure, Secondary Protein Subunits Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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