1e9m: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(23 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1e9m.gif|left|200px]]<br />
<applet load="1e9m" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1e9m, resolution 2.07&Aring;" />
'''FERREDOXIN VI FROM RHODOBACTER CAPSULATUS'''<br />


==Overview==
==Ferredoxin VI from Rhodobacter Capsulatus==
A [2Fe-2S] ferredoxin found in the photosynthetic bacterium Rhodobacter, capsulatus has been purified in recombinant form from Escherichia coli., This protein, called FdVI, resembles ferredoxins involved in iron-sulfur, cluster biosynthesis in various prokaryotic and eukaryotic cells. Purified, recombinant FdVI was recovered in high yields and appeared to be, indistinguishable from the genuine R. capsulatus ferredoxin based on, UV-visible absorption and EPR spectroscopy and mass spectrometry. FdVI has, been crystallized in the oxidized state by a sitting-drop vapour-diffusion, technique using sodium formate as precipitant. Seeding larger drops from a, previous hanging-drop-grown small crystal resulted in the formation of, long red-brown prismatic needles. Preliminary X-ray diffraction analysis, indicated that FdVI crystals are orthorhombic and belong to the space, group P2(1)2(1)2(1), with unit-cell parameters a = 45.87, b = 49.83, c =, 54.29 A.
<StructureSection load='1e9m' size='340' side='right'caption='[[1e9m]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e9m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E9M 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]] 2.07&#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=1e9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9m OCA], [https://pdbe.org/1e9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e9m RCSB], [https://www.ebi.ac.uk/pdbsum/1e9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER6_RHOCA FER6_RHOCA] Ferredoxin 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/e9/1e9m_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=1e9m ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A [2Fe-2S] ferredoxin found in the photosynthetic bacterium Rhodobacter capsulatus has been purified in recombinant form from Escherichia coli. This protein, called FdVI, resembles ferredoxins involved in iron-sulfur cluster biosynthesis in various prokaryotic and eukaryotic cells. Purified recombinant FdVI was recovered in high yields and appeared to be indistinguishable from the genuine R. capsulatus ferredoxin based on UV-visible absorption and EPR spectroscopy and mass spectrometry. FdVI has been crystallized in the oxidized state by a sitting-drop vapour-diffusion technique using sodium formate as precipitant. Seeding larger drops from a previous hanging-drop-grown small crystal resulted in the formation of long red-brown prismatic needles. Preliminary X-ray diffraction analysis indicated that FdVI crystals are orthorhombic and belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 45.87, b = 49.83, c = 54.29 A.


==About this Structure==
Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus.,Armengaud J, Sainz G, Jouanneau Y, Sieker LC Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):301-3. PMID:11173487<ref>PMID:11173487</ref>
1E9M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: FES. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E9M OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus., Armengaud J, Sainz G, Jouanneau Y, Sieker LC, Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):301-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11173487 11173487]
</div>
<div class="pdbe-citations 1e9m" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Ferredoxin|Ferredoxin]]
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
*[[Iron–sulfur proteins|Iron–sulfur proteins]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodobacter capsulatus]]
[[Category: Rhodobacter capsulatus]]
[[Category: Single protein]]
[[Category: Armengaud J]]
[[Category: Armengaud, J.]]
[[Category: Jouanneau Y]]
[[Category: Jouanneau, Y.]]
[[Category: Larry S]]
[[Category: Larry, S.]]
[[Category: Sainz G]]
[[Category: Sainz, G.]]
[[Category: Sanishvili N]]
[[Category: Sanishvili, N.]]
[[Category: Stojanoff V]]
[[Category: Stojanoff, V.]]
[[Category: FES]]
[[Category: [2fe-2s]]]
[[Category: bacterium]]
[[Category: electron transport]]
[[Category: ferredoxin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 13:32:12 2007''

Latest revision as of 11:48, 9 May 2024

Ferredoxin VI from Rhodobacter CapsulatusFerredoxin VI from Rhodobacter Capsulatus

Structural highlights

1e9m is a 1 chain structure with sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.07Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FER6_RHOCA Ferredoxin 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 PubMed

A [2Fe-2S] ferredoxin found in the photosynthetic bacterium Rhodobacter capsulatus has been purified in recombinant form from Escherichia coli. This protein, called FdVI, resembles ferredoxins involved in iron-sulfur cluster biosynthesis in various prokaryotic and eukaryotic cells. Purified recombinant FdVI was recovered in high yields and appeared to be indistinguishable from the genuine R. capsulatus ferredoxin based on UV-visible absorption and EPR spectroscopy and mass spectrometry. FdVI has been crystallized in the oxidized state by a sitting-drop vapour-diffusion technique using sodium formate as precipitant. Seeding larger drops from a previous hanging-drop-grown small crystal resulted in the formation of long red-brown prismatic needles. Preliminary X-ray diffraction analysis indicated that FdVI crystals are orthorhombic and belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 45.87, b = 49.83, c = 54.29 A.

Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus.,Armengaud J, Sainz G, Jouanneau Y, Sieker LC Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):301-3. PMID:11173487[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Armengaud J, Sainz G, Jouanneau Y, Sieker LC. Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus. Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):301-3. PMID:11173487

1e9m, resolution 2.07Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA