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3LW5

Improved model of plant photosystem I

Summary for 3LW5
Entry DOI10.2210/pdb3lw5/pdb
Related2wsc
DescriptorPhotosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit IX, Photosystem I reaction center subunit X psaK, ... (24 entities in total)
Functional Keywordsphotosynthesis, electron transfer, membrane proteins, large, 2 complexes, chlorophyll, chloroplast, chromophore, electron transport, iron, iron-sulfur, magnesium, membrane, metal-binding, photosystem i, thylakoid, transmembrane, transport
Biological sourcePisum sativum (pea)
More
Cellular locationPlastid, chloroplast thylakoid membrane ; Multi-pass membrane protein : P05310 Q9SQL2 P05311
Plastid, chloroplast thylakoid membrane : Q41038
Plastid, chloroplast thylakoid membrane ; Single-pass membrane protein : Q32904 P17227
Plastid, chloroplast thylakoid membrane ; Peripheral membrane protein ; Stromal side : P10793
Total number of polymer chains18
Total formula weight550199.73
Authors
Nelson, N.,Toporik, H. (deposition date: 2010-02-23, release date: 2010-08-18, Last modification date: 2024-11-06)
Primary citationAmunts, A.,Toporik, H.,Borovikova, A.,Nelson, N.
Structure determination and improved model of plant photosystem I
J.Biol.Chem., 285:3478-3486, 2010
Cited by
PubMed Abstract: 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.
PubMed: 19923216
DOI: 10.1074/jbc.M109.072645
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.3 Å)
Structure validation

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