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1xrd

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(New page: 200px<br /><applet load="1xrd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xrd" /> '''Light-Harvesting Complex 1 Alfa Subunit from...)
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[[Image:1xrd.gif|left|200px]]<br /><applet load="1xrd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xrd" />
 
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'''Light-Harvesting Complex 1 Alfa Subunit from Wild-Type Rhodospirillum rubrum'''<br />
 
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==Overview==
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==Light-Harvesting Complex 1 Alfa Subunit from Wild-Type Rhodospirillum rubrum==
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We have determined the solution structures of the core light-harvesting, (LH1) alpha and beta-polypeptides from wild-type purple photosynthetic, bacterium Rhodospirillum rubrum using multidimensional NMR spectroscopy., The two polypeptides form stable alpha helices in organic solution. The, structure of alpha-polypeptide consists of a long helix of 32 amino acid, residues over the central transmembrane domain and a short helical segment, at the N terminus that is followed by a three-residue loop., Pigment-coordinating histidine residue (His29) in the alpha-polypeptide is, located near the middle of the central helix. The structure of, beta-polypeptide shows a single helix of 32 amino acid residues in the, membrane-spanning region with the pigment-coordinating histidine residue, (His38) at a position close to the C-terminal end of the helix. Strong, hydrogen bonds have been identified for the backbone amide protons over, the central helical regions, indicating a rigid property of the two, polypeptides. The overall structures of the R.rubrum LH1 alpha and, beta-polypeptides are different from those previously reported for the LH1, beta-polypeptide of Rhodobacter sphaeroides, but are very similar to the, structures of the corresponding LH2 alpha and beta-polypeptides determined, by X-ray crystallography. A model constructed for the structural subunit, (B820) of LH1 complex using the solution structures reveals several, important features on the interactions between the LH1 alpha and, beta-polypeptides. The significance of the N-terminal regions of the two, polypeptides for stabilizing both B820 and LH1 complexes, as clarified by, many experiments, may be attributed to the interactions between the short, N-terminal helix (Trp2-Gln6) of alpha-polypeptide and a GxxxG motif in the, beta-polypeptide.
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<StructureSection load='1xrd' size='340' side='right'caption='[[1xrd]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xrd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XRD FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrd OCA], [https://pdbe.org/1xrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xrd RCSB], [https://www.ebi.ac.uk/pdbsum/1xrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LHA_RHORU LHA_RHORU] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xr/1xrd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1xrd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have determined the solution structures of the core light-harvesting (LH1) alpha and beta-polypeptides from wild-type purple photosynthetic bacterium Rhodospirillum rubrum using multidimensional NMR spectroscopy. The two polypeptides form stable alpha helices in organic solution. The structure of alpha-polypeptide consists of a long helix of 32 amino acid residues over the central transmembrane domain and a short helical segment at the N terminus that is followed by a three-residue loop. Pigment-coordinating histidine residue (His29) in the alpha-polypeptide is located near the middle of the central helix. The structure of beta-polypeptide shows a single helix of 32 amino acid residues in the membrane-spanning region with the pigment-coordinating histidine residue (His38) at a position close to the C-terminal end of the helix. Strong hydrogen bonds have been identified for the backbone amide protons over the central helical regions, indicating a rigid property of the two polypeptides. The overall structures of the R.rubrum LH1 alpha and beta-polypeptides are different from those previously reported for the LH1 beta-polypeptide of Rhodobacter sphaeroides, but are very similar to the structures of the corresponding LH2 alpha and beta-polypeptides determined by X-ray crystallography. A model constructed for the structural subunit (B820) of LH1 complex using the solution structures reveals several important features on the interactions between the LH1 alpha and beta-polypeptides. The significance of the N-terminal regions of the two polypeptides for stabilizing both B820 and LH1 complexes, as clarified by many experiments, may be attributed to the interactions between the short N-terminal helix (Trp2-Gln6) of alpha-polypeptide and a GxxxG motif in the beta-polypeptide.
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==About this Structure==
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Solution structures of the core light-harvesting alpha and beta polypeptides from Rhodospirillum rubrum: implications for the pigment-protein and protein-protein interactions.,Wang ZY, Gokan K, Kobayashi M, Nozawa T J Mol Biol. 2005 Mar 25;347(2):465-77. Epub 2005 Jan 25. PMID:15740753<ref>PMID:15740753</ref>
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1XRD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XRD OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Solution structures of the core light-harvesting alpha and beta polypeptides from Rhodospirillum rubrum: implications for the pigment-protein and protein-protein interactions., Wang ZY, Gokan K, Kobayashi M, Nozawa T, J Mol Biol. 2005 Mar 25;347(2):465-77. Epub 2005 Jan 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15740753 15740753]
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</div>
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<div class="pdbe-citations 1xrd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rhodospirillum rubrum]]
[[Category: Rhodospirillum rubrum]]
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[[Category: Single protein]]
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[[Category: Gokan K]]
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[[Category: Gokan, K.]]
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[[Category: Kobayashi M]]
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[[Category: Kobayashi, M.]]
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[[Category: Nozawa T]]
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[[Category: Nozawa, T.]]
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[[Category: Wang Z-Y]]
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[[Category: Wang, Z.Y.]]
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[[Category: light-harvesting]]
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[[Category: membrane spanning helix]]
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[[Category: photosynthesis]]
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[[Category: pigment binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:17:20 2007''
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Current revision

Light-Harvesting Complex 1 Alfa Subunit from Wild-Type Rhodospirillum rubrum

PDB ID 1xrd

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