1e29: Difference between revisions

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[[Image:1e29.~~gif~~|left|200px]]

[[Image:1e29.png|left|200px]]

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~~'''~~PSII ASSOCIATED CYTOCHROME C549 FROM SYNECHOCYSTIS SP.~~'''~~

===PSII ASSOCIATED CYTOCHROME C549 FROM SYNECHOCYSTIS SP.===

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_11315568}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11315568 is the PubMed ID number.

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==About this Structure==

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[[Category: Psii associated cytochrome]]

[[Category: Psii modulator]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 14~~:34:11 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:01:26 2008''

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-[[Image:1e29.gif|left|200px]]
+{{Seed}}
+[[Image:1e29.png|left|200px]]
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 {{STRUCTURE_1e29|  PDB=1e29  |  SCENE=  }}
-'''PSII ASSOCIATED CYTOCHROME C549 FROM SYNECHOCYSTIS SP.'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11315568}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11315568 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11315568}}
 ==About this Structure==
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 [[Category: Psii associated cytochrome]]
 [[Category: Psii modulator]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:34:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:01:26 2008''