1e29: Difference between revisions

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<StructureSection load='1e29' size='340' side='right'caption='[[1e29]], [[Resolution|resolution]] 1.21&Aring;' scene=''>
<StructureSection load='1e29' size='340' side='right'caption='[[1e29]], [[Resolution|resolution]] 1.21&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1e29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp Synechocystis sp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E29 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1e29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E29 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.21&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e29 OCA], [https://pdbe.org/1e29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e29 RCSB], [https://www.ebi.ac.uk/pdbsum/1e29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e29 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e29 OCA], [https://pdbe.org/1e29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e29 RCSB], [https://www.ebi.ac.uk/pdbsum/1e29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e29 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CY550_SYNY3 CY550_SYNY3]] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Required for normal function or stabilization of PSII. Extrinsic protein associated with PSII that enhances oxygen evolution.  
[https://www.uniprot.org/uniprot/CY550_SYNY3 CY550_SYNY3] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Required for normal function or stabilization of PSII. Extrinsic protein associated with PSII that enhances oxygen evolution.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e29 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e29 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:11315568</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1e29" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Synechocystis sp]]
[[Category: Synechocystis sp]]
[[Category: Coelho, R]]
[[Category: Coelho R]]
[[Category: Enguita, F J]]
[[Category: Enguita FJ]]
[[Category: Frazao, C]]
[[Category: Frazao C]]
[[Category: Sheldrick, G M]]
[[Category: Sheldrick GM]]
[[Category: Bis_histidinyl]]
[[Category: Cytochrome]]
[[Category: Electron transport]]
[[Category: Low potential]]
[[Category: Psii associated cytochrome]]
[[Category: Psii modulator]]

Revision as of 09:57, 20 March 2024

PSII associated cytochrome C549 from Synechocystis sp.

1e29, resolution 1.21Å

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