1f37: Difference between revisions

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[[Image:1f37.jpg|left|200px]]


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==STRUCTURE OF A THIOREDOXIN-LIKE [2FE-2S] FERREDOXIN FROM AQUIFEX AEOLICUS==
The line below this paragraph, containing "STRUCTURE_1f37", creates the "Structure Box" on the page.
<StructureSection load='1f37' size='340' side='right'caption='[[1f37]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1f37]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F37 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
{{STRUCTURE_1f37| PDB=1f37 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f37 OCA], [https://pdbe.org/1f37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f37 RCSB], [https://www.ebi.ac.uk/pdbsum/1f37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f37 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER2_AQUAE FER2_AQUAE] 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/f3/1f37_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=1f37 ConSurf].
<div style="clear:both"></div>


'''STRUCTURE OF A THIOREDOXIN-LIKE [2FE-2S] FERREDOXIN FROM AQUIFEX AEOLICUS'''
==See Also==
 
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The 2.3 A resolution crystal structure of a [2Fe-2S] cluster containing ferredoxin from Aquifex aeolicus reveals a thioredoxin-like fold that is novel among iron-sulfur proteins. The [2Fe-2S] cluster is located near the surface of the protein, at a site corresponding to that of the active-site disulfide bridge in thioredoxin. The four cysteine ligands are located near the ends of two surface loops. Two of these ligands can be substituted by non-native cysteine residues introduced throughout a stretch of the polypeptide chain that forms a protruding loop extending away from the cluster. The presence of homologs of this ferredoxin as components of more complex anaerobic and aerobic electron transfer systems indicates that this is a versatile fold for biological redox processes.
 
==About this Structure==
1F37 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F37 OCA].
 
==Reference==
Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus., Yeh AP, Chatelet C, Soltis SM, Kuhn P, Meyer J, Rees DC, J Mol Biol. 2000 Jul 14;300(3):587-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10884354 10884354]
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chatelet, C.]]
[[Category: Chatelet C]]
[[Category: Kuhn, P.]]
[[Category: Kuhn P]]
[[Category: Meyer, J.]]
[[Category: Meyer J]]
[[Category: Rees, D C.]]
[[Category: Rees DC]]
[[Category: Soltis, S M.]]
[[Category: Soltis SM]]
[[Category: Yeh, A P.]]
[[Category: Yeh AP]]
[[Category: Ferredoxin]]
[[Category: Thioredoxin fold]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:50:17 2008''

Latest revision as of 10:10, 7 February 2024

STRUCTURE OF A THIOREDOXIN-LIKE [2FE-2S] FERREDOXIN FROM AQUIFEX AEOLICUSSTRUCTURE OF A THIOREDOXIN-LIKE [2FE-2S] FERREDOXIN FROM AQUIFEX AEOLICUS

Structural highlights

1f37 is a 2 chain structure with sequence from Aquifex aeolicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FER2_AQUAE 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.

See Also

1f37, resolution 2.30Å

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