1V2B

Crystal Structure of PsbP Protein in the Oxygen-Evolving Complex of Photosystem II from Higher Plants

Summary for 1V2B

• Entry DOI: 10.2210/pdb1v2b/pdb
• Descriptor: 23-kDa polypeptide of photosystem II oxygen-evolving complex, alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: alpha-beta, riken structural genomics/proteomics initiative, rsgi, structural genomics, photosynthesis
• Biological source: Nicotiana tabacum (common tobacco)
• Cellular location: Plastid, chloroplast thylakoid membrane: P18212
• Total number of polymer chains: 2
• Total formula weight: 39371.26

Authors

Ifuku, K.,Nakatsu, T.,Kato, H.,Sato, F.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-10-14, release date: 2004-05-18, Last modification date: 2023-12-27)

Primary citation

Ifuku, K.,Nakatsu, T.,Kato, H.,Sato, F.
Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum
Embo Rep., 5:362-367, 2004

PubMed Abstract: PsbP 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.

PubMed: 15031714
DOI: 10.1038/sj.embor.7400113

Experimental method

X-RAY DIFFRACTION (1.6 Å)