5tis
From Proteopedia
Room temperature XFEL structure of the native, doubly-illuminated photosystem II complex
Structural highlights
Function[PSBF_THEEB] This b-type cytochrome is tightly associated with the reaction center of photosystem II and possibly is part of the water-oxidation complex (By similarity).[HAMAP-Rule:MF_00643] [PSBL_THEEB] Required for PSII activity (By similarity). [PSBC_THEEB] One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01496][1] [2] [3] [PSBJ_THEEB] This protein is a component of the reaction center of photosystem II (By similarity). [PSBB_THEEB] One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01495][4] [5] [6] [YCF12_THEEB] A core subunit of photosystem II (PSII).[HAMAP-Rule:MF_01329] [PSBU_THEEB] Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation (By similarity).[HAMAP-Rule:MF_00589] [PSBT_THEEB] Seems to play a role in the dimerization of PSII.[7] [PSBI_THEEB] This protein is a component of the reaction center of photosystem II.[HAMAP-Rule:MF_01316] [PSBA1_THEEB] This is one of the two reaction center proteins of photosystem II. [PSBX_THEEB] Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.[8] [PSBZ_THEEB] Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. May also aid in binding of PsbK, Ycf12 and the oxygen-evolving complex to PSII, at least in vitro.[9] [PSBK_THEEB] This protein is a component of the reaction center of photosystem II.[HAMAP-Rule:MF_00441] [PSBO_THEEB] MSP binds to a putative Mn-binding protein and keeps 2 of the 4 Mn-atoms associated with PSII (By similarity). [CY550_THEEB] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II. It is not essential for growth under normal conditions but is required under low CO(2) concentrations.[HAMAP-Rule:MF_01378] [PSBE_THEEB] This b-type cytochrome is tightly associated with the reaction center of photosystem II and possibly is part of the water-oxidation complex.[HAMAP-Rule:MF_00642] Publication Abstract from PubMedphenix.refine is a program within the PHENIX package that supports crystallographic structure refinement against experimental data with a wide range of upper resolution limits using a large repertoire of model parameterizations. It has several automation features and is also highly flexible. Several hundred parameters enable extensive customizations for complex use cases. Multiple user-defined refinement strategies can be applied to specific parts of the model in a single refinement run. An intuitive graphical user interface is available to guide novice users and to assist advanced users in managing refinement projects. X-ray or neutron diffraction data can be used separately or jointly in refinement. phenix.refine is tightly integrated into the PHENIX suite, where it serves as a critical component in automated model building, final structure refinement, structure validation and deposition to the wwPDB. This paper presents an overview of the major phenix.refine features, with extensive literature references for readers interested in more detailed discussions of the methods. Towards automated crystallographic structure refinement with phenix.refine.,Afonine PV, Grosse-Kunstleve RW, Echols N, Headd JJ, Moriarty NW, Mustyakimov M, Terwilliger TC, Urzhumtsev A, Zwart PH, Adams PD Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):352-67. doi:, 10.1107/S0907444912001308. Epub 2012 Mar 16. PMID:22505256[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Photosystem II | Thermosynechococcus elongatus | Adams, P D | Afonine, P V | Aller, P | Alonso-Mori, R | Andi, B | Aquila, A | Bean, M A | Bergmann, U | Boutet, S | Braeuer, P | Brewster, A S | Brunger, A T | Chatterjee, R | Cheah, M H | Dobbek, H | Docker, P T | Douthit, L | Evans, G | Fransson, T | Fuller, F | Glownia, J M | Gul, S | Hunter, M S | Hussein, R | Ibrahim, M | Kern, J | Koglin, J E | Koroidov, S | Kroll, T | Kubin, M | Laksmono, H | Lassalle, L | Liang, M | Lichtenberg, C de | Liebschner, D | Lyubimov, A Y | Messinger, J | Michels-Clark, T | Moriarty, N W | Nelson, S | Nilsson, H | Orville, A M | Pastor, E | Pham, L V | Robinson, J | Saracini, C | Sauter, N K | Seuffert, I | Shevela, D | Sierra, R G | Sikorski, M | Sokaras, D | Stan, C A | Tran, R | Uervirojnangkoorn, M | Watermann, D G | Weis, W I | Weng, T C | Weninger, C | Wernet, P | Yachandra, V K | Yano, J | Young, I D | Zhang, M | Zhu, D | Zouni, A | Zwart, P H | Electron transport | Photosynthesis | Photosystem | Room temperature | Transmembrane
