2wsf

Improved Model of Plant Photosystem I

spinqualitylabelsall models 2wsf, resolution 3.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wsf is a 10 chain structure with sequence from Arabidopsis thaliana, Glycine max, Pisum sativum and Spinacia oleracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.48Å Ligands: BCR, CLA, FRU, GLC, LMG, LMU, PQN, PRD_900003 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CAB6_ARATH The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. 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 Photosystem I functions as a sunlight energy converter, catalyzing one of the initial steps in driving oxygenic photosynthesis in cyanobacteria, algae, and higher plants. Functionally, Photosystem I captures sunlight and transfers the excitation energy through an intricate and precisely organized antenna system, consisting of a pigment network, to the center of the molecule, where it is used in the transmembrane electron transfer reaction. Our current understanding of the sophisticated mechanisms underlying these processes has profited greatly from elucidation of the crystal structures of the Photosystem I complex. In this report, we describe the developments that ultimately led to enhanced structural information of plant Photosystem I. In addition, we report an improved crystallographic model at 3.3-A resolution, which allows analysis of the structure in more detail. An improved electron density map yielded identification and tracing of subunit PsaK. The location of an additional ten beta-carotenes as well as five chlorophylls and several loop regions, which were previously uninterpretable, are now modeled. This represents the most complete plant Photosystem I structure obtained thus far, revealing the locations of and interactions among 17 protein subunits and 193 non-covalently bound photochemical cofactors. Using the new crystal structure, we examine the network of contacts among the protein subunits from the structural perspective, which provide the basis for elucidating the functional organization of the complex. Structure determination and improved model of plant photosystem I.,Amunts A, Toporik H, Borovikova A, Nelson N J Biol Chem. 2010 Jan 29;285(5):3478-86. Epub 2009 Nov 18. PMID:19923216 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Photosystem I 3D structures

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