1fxa: Difference between revisions

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New page: left|200px<br /><applet load="1fxa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fxa, resolution 2.5Å" /> '''CRYSTALLIZATION AND S...
 
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[[Image:1fxa.gif|left|200px]]<br /><applet load="1fxa" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTALLIZATION AND STRUCTURE DETERMINATION TO 2.5-ANGSTROMS RESOLUTION OF THE OXIDIZED [2FE-2S] FERREDOXIN ISOLATED FROM ANABAENA 7120'''<br />


==Overview==
==CRYSTALLIZATION AND STRUCTURE DETERMINATION TO 2.5-ANGSTROMS RESOLUTION OF THE OXIDIZED [2FE-2S] FERREDOXIN ISOLATED FROM ANABAENA 7120==
The molecular structure of the oxidized form of the [2Fe-2S] ferredoxin, isolated from the cyanobacterium Anabaena species strain PCC 7120 has been, determined by X-ray diffraction analysis to a nominal resolution of 2.5 A, and refined to a crystallographic R factor of 18.7%. Crystals used in this, investigation belong to the space group P2(1)2(1)2(1) with unit cell, dimensions of a = 37.42 A, b = 38.12 A, and c = 147.12 A and two molecules, in the asymmetric unit. The three-dimensional structure of this ferredoxin, was solved by a method that combined X-ray data from one isomorphous, heavy-atom derivative with noncrystallographic symmetry averaging and, solvent flattening. As in other plant-type [2Fe-2S] ferredoxins, the, iron-sulfur cluster is located toward the outer edge of the molecule, and, the irons are tetrahedrally coordinated by both inorganic sulfurs and, sulfurs provided by protein cysteine residues. The main secondary, structural elements include four strands of beta-pleated sheet and three, alpha-helical regions.
<StructureSection load='1fxa' size='340' side='right'caption='[[1fxa]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fxa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FXA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=1fxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxa OCA], [https://pdbe.org/1fxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fxa RCSB], [https://www.ebi.ac.uk/pdbsum/1fxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fxa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER1_NOSS1 FER1_NOSS1] 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/fx/1fxa_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=1fxa ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FXA OCA].
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120., Rypniewski WR, Breiter DR, Benning MM, Wesenberg G, Oh BH, Markley JL, Rayment I, Holden HM, Biochemistry. 1991 Apr 30;30(17):4126-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1902376 1902376]
[[Category: Large Structures]]
[[Category: Anabaena sp.]]
[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
[[Category: Single protein]]
[[Category: Benning MM]]
[[Category: Benning, M.M.]]
[[Category: Breiter DR]]
[[Category: Breiter, D.R.]]
[[Category: Holden HM]]
[[Category: Holden, H.M.]]
[[Category: Markley JL]]
[[Category: Markley, J.L.]]
[[Category: Oh B-H]]
[[Category: Oh, B.H.]]
[[Category: Rayment I]]
[[Category: Rayment, I.]]
[[Category: Rypniewski WR]]
[[Category: Rypniewski, W.R.]]
[[Category: Wesenberg G]]
[[Category: Wesenberg, G.]]
[[Category: FES]]
[[Category: electron transport]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:25:52 2007''

Latest revision as of 10:20, 7 February 2024

CRYSTALLIZATION AND STRUCTURE DETERMINATION TO 2.5-ANGSTROMS RESOLUTION OF THE OXIDIZED [2FE-2S] FERREDOXIN ISOLATED FROM ANABAENA 7120CRYSTALLIZATION AND STRUCTURE DETERMINATION TO 2.5-ANGSTROMS RESOLUTION OF THE OXIDIZED [2FE-2S] FERREDOXIN ISOLATED FROM ANABAENA 7120

Structural highlights

1fxa is a 2 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FER1_NOSS1 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

1fxa, resolution 2.50Å

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