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< | ==NMR STUDY OF 2FE-2S FERREDOXIN OF SYNECHOCOCCUS ELONGATUS== | ||
<StructureSection load='1roe' size='340' side='right'caption='[[1roe]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1roe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=1roe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1roe OCA], [https://pdbe.org/1roe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1roe RCSB], [https://www.ebi.ac.uk/pdbsum/1roe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1roe ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FER_THEVB FER_THEVB] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | |||
== 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/ro/1roe_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1roe ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ferredoxins of the [Fe2S2] type function in photosynthetic electron transport as essential electron acceptors of photosystem I. The solution structure of the 97 amino acid ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus was determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics calculations. The structure consists of a four-stranded parallel/ antiparallel beta-sheet, a short two-stranded antiparallel beta-sheet, and three short helices. The overall structure is similar to the structure of the ferredoxin from Anabaena. In contrast to related ferredoxins from mesophilic organisms, this thermostable protein contains a salt bridge inside a 17-amino acid hydrophobic core. | |||
Structure of Synechococcus elongatus [Fe2S2] ferredoxin in solution.,Baumann B, Sticht H, Scharpf M, Sutter M, Haehnel W, Rosch P Biochemistry. 1996 Oct 1;35(39):12831-41. PMID:8841126<ref>PMID:8841126</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1roe" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
[[Category: | |||
[[Category: Synechococcus elongatus]] | [[Category: Synechococcus elongatus]] | ||
[[Category: Baumann | [[Category: Baumann B]] | ||
[[Category: Haehnel | [[Category: Haehnel W]] | ||
[[Category: Roesch | [[Category: Roesch P]] | ||
[[Category: Sticht | [[Category: Sticht H]] | ||
[[Category: Sutter | [[Category: Sutter M]] | ||
Latest revision as of 12:05, 22 May 2024
NMR STUDY OF 2FE-2S FERREDOXIN OF SYNECHOCOCCUS ELONGATUSNMR STUDY OF 2FE-2S FERREDOXIN OF SYNECHOCOCCUS ELONGATUS
Structural highlights
FunctionFER_THEVB Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. 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 PubMedFerredoxins of the [Fe2S2] type function in photosynthetic electron transport as essential electron acceptors of photosystem I. The solution structure of the 97 amino acid ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus was determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics calculations. The structure consists of a four-stranded parallel/ antiparallel beta-sheet, a short two-stranded antiparallel beta-sheet, and three short helices. The overall structure is similar to the structure of the ferredoxin from Anabaena. In contrast to related ferredoxins from mesophilic organisms, this thermostable protein contains a salt bridge inside a 17-amino acid hydrophobic core. Structure of Synechococcus elongatus [Fe2S2] ferredoxin in solution.,Baumann B, Sticht H, Scharpf M, Sutter M, Haehnel W, Rosch P Biochemistry. 1996 Oct 1;35(39):12831-41. PMID:8841126[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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