1v2b
Crystal Structure of PsbP Protein in the Oxygen-Evolving Complex of Photosystem II from Higher PlantsCrystal Structure of PsbP Protein in the Oxygen-Evolving Complex of Photosystem II from Higher Plants
Structural highlights
FunctionPSBP2_TOBAC May be involved in the regulation of photosystem II. 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 PubMedPsbP is a membrane-extrinsic subunit of the water-oxidizing complex photosystem II (PS II). The evolutionary origin of PsbP has long been a mystery because it specifically exists in higher plants and green algae but not in cyanobacteria. We report here the crystal structure of PsbP from Nicotiana tabacum at a resolution of 1.6 A. Its structure is mainly composed of beta-sheet, and is not similar to any structures in cyanobacterial PS II. However, the electrostatic surface potential of PsbP is similar to that of cyanobacterial PsbV (cyt c(550)), which has a function similar to PsbP. A structural homology search with the DALI algorithm indicated that the folding of PsbP is very similar to that of Mog1p, a regulatory protein for the nuclear transport of Ran GTPase. The structure of PsbP provides insight into its novel function in GTP-regulated metabolism in PS II. Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum.,Ifuku K, Nakatsu T, Kato H, Sato F EMBO Rep. 2004 Apr;5(4):362-7. Epub 2004 Mar 12. PMID:15031714[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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