1xrd
From Proteopedia
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'''Light-Harvesting Complex 1 Alfa Subunit from Wild-Type Rhodospirillum rubrum''' | '''Light-Harvesting Complex 1 Alfa Subunit from Wild-Type Rhodospirillum rubrum''' | ||
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[[Category: Nozawa, T.]] | [[Category: Nozawa, T.]] | ||
[[Category: Wang, Z Y.]] | [[Category: Wang, Z Y.]] | ||
| - | [[Category: | + | [[Category: Light-harvesting]] |
| - | [[Category: | + | [[Category: Membrane spanning helix]] |
| - | [[Category: | + | [[Category: Photosynthesis]] |
| - | [[Category: | + | [[Category: Pigment binding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:24:36 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:24, 3 May 2008
Light-Harvesting Complex 1 Alfa Subunit from Wild-Type Rhodospirillum rubrum
Overview
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.
About this Structure
1XRD is a Single protein structure of sequence from Rhodospirillum rubrum. Full crystallographic 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 Sat May 3 15:24:36 2008
