1jo5: Difference between revisions

Revision as of 20:32, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jo5.png

Template:STRUCTURE 1jo5

Rhodobacter sphaeroides Light Harvesting 1 beta Subunit in Detergent MicellesRhodobacter sphaeroides Light Harvesting 1 beta Subunit in Detergent Micelles

Template:ABSTRACT PUBMED 11772000

About this StructureAbout this Structure

1JO5 is a Single protein structure of sequence from Rhodobacter sphaeroides. Full experimental information is available from OCA.

ReferenceReference

Structure of the Rhodobacter sphaeroides light-harvesting 1 beta subunit in detergent micelles., Sorgen PL, Cahill SM, Krueger-Koplin RD, Krueger-Koplin ST, Schenck CC, Girvin ME, Biochemistry. 2002 Jan 8;41(1):31-41. PMID:11772000

Page seeded by OCA on Tue Jul 1 20:32:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1jo5.jpg|left|200px]]
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 {{STRUCTURE_1jo5|  PDB=1jo5  |  SCENE=  }}
-'''Rhodobacter sphaeroides Light Harvesting 1 beta Subunit in Detergent Micelles'''
+===Rhodobacter sphaeroides Light Harvesting 1 beta Subunit in Detergent Micelles===
-==Overview==
+<!--
-The light harvesting 1 antenna (LH1) complex from Rhodobacter sphaeroides funnels excitation energy to the photosynthetic reaction center. Our ultimate goal is to build up the structure of LH1 from structures of its individual subunits, much as the antenna can self-assemble from its components in membrane-mimicking detergent micelles. The beta subunit adopts a nativelike conformation in Zwittergent 3:12 micelles as demonstrated by its ability to take the first step of assembly, binding BChl a. Multidimensional NMR spectroscopy shows that the beta subunit folds as a helix((L12-S25))-hinge((G26-W28))-helix((L29-W44)) structure with the helical regions for the 10 lowest-energy structures having backbone rmsds of 0.26 and 0.24 A, respectively. Mn(2+) relaxation data and the protein-detergent NOE pattern show the C-terminal helix embedded in the micelle and the N-terminal helix lying along the detergent micelle surface with a 60 degrees angle between their long axes. (15)N relaxation data for residues L12-W44 are typical of a well-ordered protein with a correlation time of 8.25 +/- 2.1 ns. The presence of the hinge region placing the N-terminal helix along the membrane surface may be the structural feature responsible for the functional differences observed between the LH1 and LH2 beta subunits.
+The line below this paragraph, {{ABSTRACT_PUBMED_11772000}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11772000 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11772000}}
 ==About this Structure==
-JO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO5 OCA].
+JO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO5 OCA].
 ==Reference==
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 [[Category: Helix-turn-helix]]
 [[Category: Membrane protein]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 20:32:31 2008''