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1xrd

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{{STRUCTURE_1xrd| PDB=1xrd | SCENE= }}
{{STRUCTURE_1xrd| PDB=1xrd | SCENE= }}
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'''Light-Harvesting Complex 1 Alfa Subunit from Wild-Type Rhodospirillum rubrum'''
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===Light-Harvesting Complex 1 Alfa 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.
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{{ABSTRACT_PUBMED_15740753}}
==About this Structure==
==About this Structure==
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1XRD 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=1XRD OCA].
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1XRD 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=1XRD OCA].
==Reference==
==Reference==
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[[Category: Photosynthesis]]
[[Category: Photosynthesis]]
[[Category: Pigment binding]]
[[Category: Pigment binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:24:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:14:35 2008''

Revision as of 03:14, 29 July 2008

Image:1xrd.png

Template:STRUCTURE 1xrd

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

Template:ABSTRACT PUBMED 15740753

About this Structure

1XRD 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 Tue Jul 29 06:14:35 2008

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