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| | {{STRUCTURE_1wrg| PDB=1wrg | SCENE= }} | | {{STRUCTURE_1wrg| PDB=1wrg | SCENE= }} |
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| - | '''Light-Harvesting Complex 1 Beta Subunit from Wild-Type Rhodospirillum rubrum'''
| + | ===Light-Harvesting Complex 1 Beta Subunit from Wild-Type Rhodospirillum rubrum=== |
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| - | ==Overview==
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15740753}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15740753 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15740753}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1WRG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRG OCA]. | + | 1WRG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRG OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Photosynthesis]] | | [[Category: Photosynthesis]] |
| | [[Category: Pigment binding]] | | [[Category: Pigment binding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:02:58 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:01:57 2008'' |
Revision as of 14:02, 28 July 2008
Template:STRUCTURE 1wrg
Light-Harvesting Complex 1 Beta Subunit from Wild-Type Rhodospirillum rubrum
Template:ABSTRACT PUBMED 15740753
About this Structure
1WRG is a Single protein structure of sequence from Rhodospirillum rubrum. Full experimental information is available from OCA.
Reference
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
Page seeded by OCA on Mon Jul 28 17:01:57 2008
