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2JBL

PHOTOSYNTHETIC REACTION CENTER FROM BLASTOCHLORIS VIRIDIS

Replaces:  4PRC
Summary for 2JBL
Entry DOI10.2210/pdb2jbl/pdb
Related1DXR 1PRC 1R2C 1VRN 2PRC 3PRC 5PRC 6PRC 7PRC
DescriptorPHOTOSYNTHETIC REACTION CENTER CYTOCHROME C SUBUNIT, STIGMATELLIN A, FE (III) ION, ... (14 entities in total)
Functional Keywordschromophore, formylation, chlorophyll, lipoprotein, stigmatellin, metal-binding, transmembrane, iron, heme, membrane, transport, magnesium, photosynthesis, reaction center, electron transport, bacteriochlorophyll, photosynthetic reaction center
Biological sourceBLASTOCHLORIS VIRIDIS (RHODOPSEUDOMONAS VIRIDIS)
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Total number of polymer chains4
Total formula weight145785.34
Authors
Lancaster, C.R.D. (deposition date: 2006-12-08, release date: 2007-03-13, Last modification date: 2024-11-20)
Primary citationLancaster, C.R.D.,Hunte, C.,Kelley, J.,Trumpower, B.L.,Ditchfield, R.
A Comparison of Stigmatellin Conformations, Free and Bound to the Photosynthetic Reaction Center and the Cytochrome Bc(1) Complex.
J.Mol.Biol., 368:197-, 2007
Cited by
PubMed Abstract: We describe in detail the conformations of the inhibitor stigmatellin in its free form and bound to the ubiquinone-reducing (Q(B)) site of the reaction center and to the ubiquinol-oxidizing (Q(o)) site of the cytochrome bc(1) complex. We present here the first structures of a stereochemically correct stigmatellin in complexes with a bacterial reaction center and the yeast cytochrome bc1 complex. The conformations of the inhibitor bound to the two enzymes are not the same. We focus on the orientations of the stigmatellin side-chain relative to the chromone head group, and on the interaction of the stigmatellin side-chain with these membrane protein complexes. The different conformations of stigmatellin found illustrate the structural variability of the Q sites, which are affected by the same inhibitor. The free rotation about the chi1 dihedral angle is an essential factor for allowing stigmatellin to bind in both the reaction center and the cytochrome bc1 pocket.
PubMed: 17337272
DOI: 10.1016/J.JMB.2007.02.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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