1e29
From Proteopedia
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|PDB= 1e29 |SIZE=350|CAPTION= <scene name='initialview01'>1e29</scene>, resolution 1.21Å | |PDB= 1e29 |SIZE=350|CAPTION= <scene name='initialview01'>1e29</scene>, resolution 1.21Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e29 OCA], [http://www.ebi.ac.uk/pdbsum/1e29 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e29 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Frazao, C.]] | [[Category: Frazao, C.]] | ||
[[Category: Sheldrick, G M.]] | [[Category: Sheldrick, G M.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: HEC]] | ||
[[Category: bis_histidinyl]] | [[Category: bis_histidinyl]] | ||
[[Category: cytochrome]] | [[Category: cytochrome]] | ||
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[[Category: psii modulator]] | [[Category: psii modulator]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:53:30 2008'' |
Revision as of 16:53, 30 March 2008
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| , resolution 1.21Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.. 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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