1jo5: Difference between revisions

New page: left|200px<br /><applet load="1jo5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jo5" /> '''Rhodobacter sphaeroides Light Harvesting 1 b...
 
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1jo5.jpg|left|200px]]<br /><applet load="1jo5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jo5" />
'''Rhodobacter sphaeroides Light Harvesting 1 beta Subunit in Detergent Micelles'''<br />


==Overview==
==Rhodobacter sphaeroides Light Harvesting 1 beta Subunit in Detergent Micelles==
The light harvesting 1 antenna (LH1) complex from Rhodobacter sphaeroides, funnels excitation energy to the photosynthetic reaction center. Our, ultimate goal is to build up the structure of LH1 from structures of its, individual subunits, much as the antenna can self-assemble from its, components in membrane-mimicking detergent micelles. The beta subunit, adopts a nativelike conformation in Zwittergent 3:12 micelles as, demonstrated by its ability to take the first step of assembly, binding, BChl a. Multidimensional NMR spectroscopy shows that the beta subunit, folds as a helix((L12-S25))-hinge((G26-W28))-helix((L29-W44)) structure, with the helical regions for the 10 lowest-energy structures having, backbone rmsds of 0.26 and 0.24 A, respectively. Mn(2+) relaxation data, and the protein-detergent NOE pattern show the C-terminal helix embedded, in the micelle and the N-terminal helix lying along the detergent micelle, surface with a 60 degrees angle between their long axes. (15)N relaxation, data for residues L12-W44 are typical of a well-ordered protein with a, correlation time of 8.25 +/- 2.1 ns. The presence of the hinge region, placing the N-terminal helix along the membrane surface may be the, structural feature responsible for the functional differences observed, between the LH1 and LH2 beta subunits.
<StructureSection load='1jo5' size='340' side='right'caption='[[1jo5]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jo5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JO5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1jo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jo5 OCA], [https://pdbe.org/1jo5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jo5 RCSB], [https://www.ebi.ac.uk/pdbsum/1jo5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jo5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LHB1_CERSP LHB1_CERSP] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jo/1jo5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jo5 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The light harvesting 1 antenna (LH1) complex from Rhodobacter sphaeroides funnels excitation energy to the photosynthetic reaction center. Our ultimate goal is to build up the structure of LH1 from structures of its individual subunits, much as the antenna can self-assemble from its components in membrane-mimicking detergent micelles. The beta subunit adopts a nativelike conformation in Zwittergent 3:12 micelles as demonstrated by its ability to take the first step of assembly, binding BChl a. Multidimensional NMR spectroscopy shows that the beta subunit folds as a helix((L12-S25))-hinge((G26-W28))-helix((L29-W44)) structure with the helical regions for the 10 lowest-energy structures having backbone rmsds of 0.26 and 0.24 A, respectively. Mn(2+) relaxation data and the protein-detergent NOE pattern show the C-terminal helix embedded in the micelle and the N-terminal helix lying along the detergent micelle surface with a 60 degrees angle between their long axes. (15)N relaxation data for residues L12-W44 are typical of a well-ordered protein with a correlation time of 8.25 +/- 2.1 ns. The presence of the hinge region placing the N-terminal helix along the membrane surface may be the structural feature responsible for the functional differences observed between the LH1 and LH2 beta subunits.


==About this Structure==
Structure of the Rhodobacter sphaeroides light-harvesting 1 beta subunit in detergent micelles.,Sorgen PL, Cahill SM, Krueger-Koplin RD, Krueger-Koplin ST, Schenck CC, Girvin ME Biochemistry. 2002 Jan 8;41(1):31-41. PMID:11772000<ref>PMID:11772000</ref>
1JO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JO5 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of the Rhodobacter sphaeroides light-harvesting 1 beta subunit in detergent micelles., Sorgen PL, Cahill SM, Krueger-Koplin RD, Krueger-Koplin ST, Schenck CC, Girvin ME, Biochemistry. 2002 Jan 8;41(1):31-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11772000 11772000]
</div>
[[Category: Rhodobacter sphaeroides]]
<div class="pdbe-citations 1jo5" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Cahill, S.M.]]
<references/>
[[Category: Girvin, M.E.]]
__TOC__
[[Category: Krueger-Koplin, R.D.]]
</StructureSection>
[[Category: Krueger-Koplin, S.T.]]
[[Category: Cereibacter sphaeroides]]
[[Category: Schenck, C.G.]]
[[Category: Large Structures]]
[[Category: Sorgen, P.L.]]
[[Category: Cahill SM]]
[[Category: detergent micelle]]
[[Category: Girvin ME]]
[[Category: helix-turn-helix]]
[[Category: Krueger-Koplin RD]]
[[Category: membrane protein]]
[[Category: Krueger-Koplin ST]]
 
[[Category: Schenck CG]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:25:00 2007''
[[Category: Sorgen PL]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA