1nw0: Difference between revisions
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<StructureSection load='1nw0' size='340' side='right'caption='[[1nw0]]' scene=''> | <StructureSection load='1nw0' size='340' side='right'caption='[[1nw0]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NW0 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nw0 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1nw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nw0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Latest revision as of 10:06, 25 August 2021
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MODEL OF THE B820 FORM OF THE LIGHT-HARVESTING COMPLEX I FROM RHODOSPIRILLUM RUBRUMMODEL OF THE B820 FORM OF THE LIGHT-HARVESTING COMPLEX I FROM RHODOSPIRILLUM RUBRUM
Structural highlights
Publication Abstract from PubMedThe effect of partial digestion by trypsin and GluC protease on the association of the membrane polypeptides of LH1 from Rhodospirillum (Rsp.) rubrum was studied. Trypsin and GluC protease treatments of LH1 result in the cleavage of the first three amino acids from the alpha polypeptide and of the first 18 amino acids from the beta polypeptide, respectively, without any noticeable reorganization of their secondary structure, as measured by attenuated total reflectance Fourier transform IR spectroscopy. However, the enthalpy variation accompanying dimer formation was dramatically reduced by the protease attacks by as much as 80%. Our results show that the alphabeta heterodimer is mainly stabilized by hydrophobic interactions which involve the amino-terminal extensions of the participating polypeptides. Using the close homology between the polypeptides of Rsp. rubrum LH1 and that of Rsp. molischianum LH2, whose structure is known, a structural model for these "hydrophobic pockets" lying close to the membrane interface is proposed. Hydrophobic pockets at the membrane interface: an original mechanism for membrane protein interactions.,Arluison V, Seguin J, Le Caer JP, Sturgis JN, Robert B Biochemistry. 2004 Feb 10;43(5):1276-82. PMID:14756563[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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