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PDBsum entry 1zrt
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Electron transport
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PDB id
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1zrt
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Contents |
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431 a.a.
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248 a.a.
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183 a.a.
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References listed in PDB file
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Key reference
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Title
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X-Ray structure of rhodobacter capsulatus cytochrome bc (1): comparison with its mitochondrial and chloroplast counterparts.
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Authors
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E.A.Berry,
L.S.Huang,
L.K.Saechao,
N.G.Pon,
M.Valkova-Valchanova,
F.Daldal.
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Ref.
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Photosynth Res, 2004,
81,
251-275.
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PubMed id
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Abstract
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Ubihydroquinone: cytochrome (cyt)c oxidoreductase, or cyt bc (1), is a
widespread, membrane integral enzyme that plays a crucial role during
photosynthesis and respiration. It is one of the major contributors of the
electrochemical proton gradient, which is subsequently used for ATP synthesis.
The simplest form of the cyt bc (1) is found in bacteria, and it contains only
the three ubiquitously conserved catalytic subunits: the Fe-S protein, cyt b and
cyt c (1). Here we present a preliminary X-ray structure of Rhodobacter
capsulatus cyt bc (1) at 3.8 A and compare it to the available structures of its
homologues from mitochondria and chloroplast. Using the bacterial enzyme
structure, we highlight the structural similarities and differences that are
found among the three catalytic subunits between the members of this family of
enzymes. In addition, we discuss the locations of currently known critical
mutations, and their implications in terms of the cyt bc (1) catalysis.
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