1rgn: Difference between revisions

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New page: left|200px<br /><applet load="1rgn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rgn, resolution 2.80Å" /> '''Structure of the rea...
 
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'''Structure of the reaction centre from Rhodobacter sphaeroides carotenoidless strain R-26.1 reconstituted with spheroidene'''<br />
'''Structure of the reaction centre from Rhodobacter sphaeroides carotenoidless strain R-26.1 reconstituted with spheroidene'''<br />


==Overview==
==Overview==
X-ray diffraction was used to determine high-resolution structures of the, reaction center (RC) complex from the carotenoidless mutant, Rb., sphaeroides R-26.1, without or reconstituted with carotenoids. The results, are compared with the structure of the RC from a semiaerobically grown Rb., sphaeroides strain 2.4.1. The investigation reveals the structure of the, carotenoid in the different protein preparations, the nature of its, binding site, and a plausible mechanism by which the carotenoid is, incorporated unidirectionally in its characteristic geometric, configuration. The structural data suggest that the accessibility of the, carotenoid to the binding site is controlled by a specific "gatekeeper", residue which allows the carotenoid to approach the binding site from only, one direction. Carotenoid binding to the protein is secured by hydrogen, bonding to a separate "locking" amino acid. The study reveals the specific, molecular interactions that control how the carotenoid protects the, photosynthetic apparatus against photo-induced oxidative destruction.
X-ray diffraction was used to determine high-resolution structures of the reaction center (RC) complex from the carotenoidless mutant, Rb. sphaeroides R-26.1, without or reconstituted with carotenoids. The results are compared with the structure of the RC from a semiaerobically grown Rb. sphaeroides strain 2.4.1. The investigation reveals the structure of the carotenoid in the different protein preparations, the nature of its binding site, and a plausible mechanism by which the carotenoid is incorporated unidirectionally in its characteristic geometric configuration. The structural data suggest that the accessibility of the carotenoid to the binding site is controlled by a specific "gatekeeper" residue which allows the carotenoid to approach the binding site from only one direction. Carotenoid binding to the protein is secured by hydrogen bonding to a separate "locking" amino acid. The study reveals the specific molecular interactions that control how the carotenoid protects the photosynthetic apparatus against photo-induced oxidative destruction.


==About this Structure==
==About this Structure==
1RGN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with FE, PO4, BCL, BPH, U10, SPO and LDA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RGN OCA].  
1RGN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=BCL:'>BCL</scene>, <scene name='pdbligand=BPH:'>BPH</scene>, <scene name='pdbligand=U10:'>U10</scene>, <scene name='pdbligand=SPO:'>SPO</scene> and <scene name='pdbligand=LDA:'>LDA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGN OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rhodobacter sphaeroides]]
[[Category: Rhodobacter sphaeroides]]
[[Category: Cogdell, R.J.]]
[[Category: Cogdell, R J.]]
[[Category: Frank, H.A.]]
[[Category: Frank, H A.]]
[[Category: Isaacs, N.W.]]
[[Category: Isaacs, N W.]]
[[Category: McKendrick, K.]]
[[Category: McKendrick, K.]]
[[Category: Mitchell, I.A.]]
[[Category: Mitchell, I A.]]
[[Category: Roszak, A.W.]]
[[Category: Roszak, A W.]]
[[Category: BCL]]
[[Category: BCL]]
[[Category: BPH]]
[[Category: BPH]]
Line 32: Line 32:
[[Category: reconstituted carotenoid]]
[[Category: reconstituted carotenoid]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:35:00 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:40 2008''

Revision as of 15:50, 21 February 2008

File:1rgn.gif


1rgn, resolution 2.80Å

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Structure of the reaction centre from Rhodobacter sphaeroides carotenoidless strain R-26.1 reconstituted with spheroidene

OverviewOverview

X-ray diffraction was used to determine high-resolution structures of the reaction center (RC) complex from the carotenoidless mutant, Rb. sphaeroides R-26.1, without or reconstituted with carotenoids. The results are compared with the structure of the RC from a semiaerobically grown Rb. sphaeroides strain 2.4.1. The investigation reveals the structure of the carotenoid in the different protein preparations, the nature of its binding site, and a plausible mechanism by which the carotenoid is incorporated unidirectionally in its characteristic geometric configuration. The structural data suggest that the accessibility of the carotenoid to the binding site is controlled by a specific "gatekeeper" residue which allows the carotenoid to approach the binding site from only one direction. Carotenoid binding to the protein is secured by hydrogen bonding to a separate "locking" amino acid. The study reveals the specific molecular interactions that control how the carotenoid protects the photosynthetic apparatus against photo-induced oxidative destruction.

About this StructureAbout this Structure

1RGN is a Protein complex structure of sequences from Rhodobacter sphaeroides with , , , , , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Protein regulation of carotenoid binding; gatekeeper and locking amino acid residues in reaction centers of Rhodobacter sphaeroides., Roszak AW, McKendrick K, Gardiner AT, Mitchell IA, Isaacs NW, Cogdell RJ, Hashimoto H, Frank HA, Structure. 2004 May;12(5):765-73. PMID:15130469

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