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PDBsum entry 1e29
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Electron transport
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PDB id
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1e29
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of low-Potential cytochrome c549 from synechocystis sp. Pcc 6803 at 1.21 a resolution.
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Authors
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C.Frazão,
F.J.Enguita,
R.Coelho,
G.M.Sheldrick,
J.A.Navarro,
M.Hervás,
M.A.De la rosa,
M.A.Carrondo.
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Ref.
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J Biol Inorg Chem, 2001,
6,
324-332.
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PubMed id
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Abstract
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The crystal structure of low-potential cytochrome c549, an extrinsic component
of the photosystem II (PS II) from Synechocystis sp. PCC 6803, was obtained
directly from single-wavelength 1.21 A resolution diffraction data. This is the
first monodomain bis-histidinyl monoheme cytochrome c to be structurally
characterized. The extended N-terminal region of c549 builds up a two-strand
antiparallel beta-sheet in a hairpin motif, which extends through two molecules
owing to crystal packing. Both peptide termini are involved in crystal contacts,
which may explain their protrusion out of the globular fold. The C-terminus is
preceded by a 9 A-long hydrophobic finger extending from a positively charged
base and could be involved in PSII interactions, as well as a protruding
negative patch built by a set of conserved acidic residues among c549 sequences.
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