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10.1016/j.str.2014.05.004 http://scihub22266oqcxt.onion/10.1016/j.str.2014.05.004 C4105968!4105968!24931468     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Structure 2014 ; 22 (7): 1008-15 Nephropedia Template TP {{tp|p=24931468|t=2014. Internal Lipid Architecture of the Hetero-Oligomeric Cytochrome b6f Complex |pdf=|usr=}}{{24931468}} gab.com Text Internal Lipid Architecture of the Hetero-Oligomeric Cytochrome b6f Complex JO: Structure http://www.kidney.de/pget.php?&tw=1&pmid=24931468 #FOAvip The role of lipids in the assembly, structure and function of hetero-oligomeric membrane protein complexes is poorly understood. The photosynthetic cytochrome b6f complex, a 16-mer of eight distinct subunits and 26 trans-membrane helices, catalyzes trans-membrane proton-coupled electron transfer for energy storage. Using a 2.5 Å crystal structure of the dimeric complex, 23 distinct lipid binding sites per monomer have been identified in the present study. Annular lipids are proposed to provide a connection for (i) super-complex formation with the photosystem-I reaction center, and (ii) the LHCII kinase enzyme for trans-membrane signaling. Internal lipids mediate (iii) cross-linking to stabilize the domain-swapped iron-sulfur protein subunit, (iv) dielectric heterogeneity within inter-monomer and intra-monomer electron transfer pathways, and (v) dimer stabilization through lipid-mediated inter-monomer interactions. This study provides the most complete structure-analysis thus far obtained of lipid-mediated functions in a multi-subunit membrane protein complex, and reveals lipid-sites at positions essential for assembly and function. Twit Text FOAVip Internal Lipid Architecture of the Hetero-Oligomeric Cytochrome b6f Complex ????Structure http://www.kidney.de/pget.php?&tw=1&pmid=24931468 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24931468 #FOAvip English Wikipedia <ref>{{Cite pmid|24931468}}</ref> Internal Lipid Architecture of the Hetero-Oligomeric Cytochrome b6f Complex #MMPMID24931468 Hasan SS; Cramer WA Structure 2014[Jul]; 22 (7): 1008-15 PMID24931468show ga The role of lipids in the assembly, structure and function of hetero-oligomeric membrane protein complexes is poorly understood. The photosynthetic cytochrome b6f complex, a 16-mer of eight distinct subunits and 26 trans-membrane helices, catalyzes trans-membrane proton-coupled electron transfer for energy storage. Using a 2.5 Å crystal structure of the dimeric complex, 23 distinct lipid binding sites per monomer have been identified in the present study. Annular lipids are proposed to provide a connection for (i) super-complex formation with the photosystem-I reaction center, and (ii) the LHCII kinase enzyme for trans-membrane signaling. Internal lipids mediate (iii) cross-linking to stabilize the domain-swapped iron-sulfur protein subunit, (iv) dielectric heterogeneity within inter-monomer and intra-monomer electron transfer pathways, and (v) dimer stabilization through lipid-mediated inter-monomer interactions. This study provides the most complete structure-analysis thus far obtained of lipid-mediated functions in a multi-subunit membrane protein complex, and reveals lipid-sites at positions essential for assembly and function. äInternal Lipid Architecture of the Hetero-Oligomeric Cytochrome b6f Co(epmc).pdf DeepDyve Pubget Overpricing