1pse

THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF PSAE FROM THE CYANOBACTERIUM SYNECHOCOCCUS SP. STRAIN PCC 7002: A PHOTOSYSTEM I PROTEIN THAT SHOWS STRUCTURAL HOMOLOGY WITH SH3 DOMAINS

spinqualitylabelsall models 1pse, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pse is a 1 chain structure with sequence from Agmenellum quadruplicatum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1psf Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PSAE_SYNP2] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase. 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 PubMed PsaE is a 69 amino acid polypeptide from photosystem I present on the stromal side of the thylakoid membrane. The three-dimensional solution structure of this protein from the cyanobacterium Synechococcus sp. strain PCC 7002 was determined at pH 5.8 and room temperature using over 900 experimental restraints derived from two- and three-dimensional NMR experiments. The structure is comprised of a well-defined five-stranded beta-sheet with (+1, +1, +1, -4 alpha) topology. There is no helical region except for a single turn of 3(10) helix between the beta D and beta E strands. PsaE also exhibits a large unrestrained loop spanning residues 42-56. A comparison to known protein structures revealed similarity with the Src homology 3 (SH3) domain, a membrane-associated protein involved in signal transduction in eukaryotes. The match is remarkable as 47 of the alpha-carbons of PsaE can be superimposed onto those of the SH3 domain from chicken brain alpha-spectrin with a root-mean-square deviation of 2.3 A. Although the amino acid sequences have low identity and the loops are different in both proteins, the topology of the beta-sheet and the 3(10) turn is conserved. SH3 domains from other sources show a similar structural homology. The structure of PsaE was used to suggest approaches for elucidating its roles within photosystem I. Three-dimensional solution structure of PsaE from the cyanobacterium Synechococcus sp. strain PCC 7002, a photosystem I protein that shows structural homology with SH3 domains.,Falzone CJ, Kao YH, Zhao J, Bryant DA, Lecomte JT Biochemistry. 1994 May 24;33(20):6052-62. PMID:8193119 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Photosystem I

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