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==THE SOLUTION NMR STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN ALGA MONORAPHIDIUM BRAUNII, MINIMIZED AVERAGE STRUCTURE== | |||
<StructureSection load='1a2s' size='340' side='right'caption='[[1a2s]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1a2s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorolobion_braunii Chlorolobion braunii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2S FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1a2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2s OCA], [https://pdbe.org/1a2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2s RCSB], [https://www.ebi.ac.uk/pdbsum/1a2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CYC6_CHLBR CYC6_CHLBR] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a2/1a2s_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1a2s ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cytochrome c6 from Monoraphidium braunii, an 89-amino acid electron transfer protein, has been investigated by NMR in solution, in its oxidized form, at pH 7 and 300 K. By using a combination of COSY, TOCSY, and NOESY experiments, 84% of the proton resonances have been assigned. A total of 1668 experimental NOE constraints, 1109 of which were meaningful, together with 288 pseudocontact shifts, have been used to determine the structure in solution. This is represented as a family of 40 structures which have been energy minimized. The rmsd values with respect to the mean structure are 0.57 +/- 0.08 and 0.94 +/- 0.09 A for the backbone and heavy atoms, respectively. The structure has been found to be very similar to that of the reduced form, except for a rearrangement in propionate 7, a feature which has been observed in all c-type cytochromes investigated so far. Such a feature could be relevant for the efficiency of the electron transfer pathway with either the oxidizing or the reducing partners. Other differences in the oxidation states have been noted in the region proposed to be involved in the interaction with the physiological partners. | |||
Solution structure of oxidized cytochrome c6 from the green alga Monoraphidium braunii.,Banci L, Bertini I, De la Rosa MA, Koulougliotis D, Navarro JA, Walter O Biochemistry. 1998 Apr 7;37(14):4831-43. PMID:9538000<ref>PMID:9538000</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1a2s" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Chlorolobion braunii]] | |||
== | [[Category: Large Structures]] | ||
< | [[Category: Banci L]] | ||
[[Category: | [[Category: Bertini I]] | ||
[[Category: | [[Category: De La Rosa MA]] | ||
[[Category: | [[Category: Koulougliotis D]] | ||
[[Category: | [[Category: Navarro JA]] | ||
[[Category: Walter O]] | |||
[[Category: | |||
[[Category: | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 09:21, 30 October 2024
THE SOLUTION NMR STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN ALGA MONORAPHIDIUM BRAUNII, MINIMIZED AVERAGE STRUCTURETHE SOLUTION NMR STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN ALGA MONORAPHIDIUM BRAUNII, MINIMIZED AVERAGE STRUCTURE
Structural highlights
FunctionCYC6_CHLBR Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCytochrome c6 from Monoraphidium braunii, an 89-amino acid electron transfer protein, has been investigated by NMR in solution, in its oxidized form, at pH 7 and 300 K. By using a combination of COSY, TOCSY, and NOESY experiments, 84% of the proton resonances have been assigned. A total of 1668 experimental NOE constraints, 1109 of which were meaningful, together with 288 pseudocontact shifts, have been used to determine the structure in solution. This is represented as a family of 40 structures which have been energy minimized. The rmsd values with respect to the mean structure are 0.57 +/- 0.08 and 0.94 +/- 0.09 A for the backbone and heavy atoms, respectively. The structure has been found to be very similar to that of the reduced form, except for a rearrangement in propionate 7, a feature which has been observed in all c-type cytochromes investigated so far. Such a feature could be relevant for the efficiency of the electron transfer pathway with either the oxidizing or the reducing partners. Other differences in the oxidation states have been noted in the region proposed to be involved in the interaction with the physiological partners. Solution structure of oxidized cytochrome c6 from the green alga Monoraphidium braunii.,Banci L, Bertini I, De la Rosa MA, Koulougliotis D, Navarro JA, Walter O Biochemistry. 1998 Apr 7;37(14):4831-43. PMID:9538000[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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