1e29

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(New page: 200px<br /><applet load="1e29" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e29, resolution 1.21&Aring;" /> '''PSII ASSOCIATED CYTO...)
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[[Image:1e29.gif|left|200px]]<br /><applet load="1e29" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1e29.gif|left|200px]]<br /><applet load="1e29" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1e29, resolution 1.21&Aring;" />
caption="1e29, resolution 1.21&Aring;" />
'''PSII ASSOCIATED CYTOCHROME C549 FROM SYNECHOCYSTIS SP.'''<br />
'''PSII ASSOCIATED CYTOCHROME C549 FROM SYNECHOCYSTIS SP.'''<br />
==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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1E29 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with CA and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E29 OCA].
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1E29 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E29 OCA].
==Reference==
==Reference==
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[[Category: Synechocystis sp.]]
[[Category: Synechocystis sp.]]
[[Category: Coelho, R.]]
[[Category: Coelho, R.]]
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[[Category: Enguita, F.J.]]
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[[Category: Enguita, F J.]]
[[Category: Frazao, C.]]
[[Category: Frazao, C.]]
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[[Category: Sheldrick, G.M.]]
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[[Category: Sheldrick, G M.]]
[[Category: CA]]
[[Category: CA]]
[[Category: HEC]]
[[Category: HEC]]
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[[Category: psii modulator]]
[[Category: psii modulator]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:44:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:01 2008''

Revision as of 10:23, 21 February 2008


1e29, resolution 1.21Å

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PSII ASSOCIATED CYTOCHROME C549 FROM SYNECHOCYSTIS SP.

Overview

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.

About this Structure

1E29 is a Single protein structure of sequence from Synechocystis sp. with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of low-potential cytochrome c549 from Synechocystis sp. PCC 6803 at 1.21 A resolution., Frazao C, Enguita FJ, Coelho R, Sheldrick GM, Navarro JA, Hervas M, De la Rosa MA, Carrondo MA, J Biol Inorg Chem. 2001 Mar;6(3):324-32. PMID:11315568

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