1l5p: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
New page: left|200px<br /><applet load="1l5p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l5p, resolution 2.2Å" /> '''Crystal Structure of ...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1l5p.jpg|left|200px]]<br /><applet load="1l5p" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1l5p, resolution 2.2&Aring;" />
'''Crystal Structure of Trichomonas vaginalis Ferredoxin'''<br />


==Overview==
==Crystal Structure of Trichomonas vaginalis Ferredoxin==
Crystallographic studies revealing the three-dimensional structure of the, oxidized form of the [2Fe-2S] ferredoxin from Trichomonas vaginalis (TvFd), are presented. TvFd, a member of the hydrogenosomal class of ferredoxins, possesses a unique combination of redox and spectroscopic properties, and, is believed to be the biological molecule that activates the drug, metronidazole reductively in the treatment of trichomoniasis. It is the, first hydrogenosomal ferredoxin to have its structure determined. The, structure of TvFd reveals a monomeric, 93 residue protein with a fold, similar to that of other known [2Fe-2S] ferredoxins. It contains nine, hydrogen bonds to the sulfur atoms of the cluster, which is more than the, number predicted on the basis of the spectroscopic data. The TvFd, structure contains a large dipole moment like adrenodoxin, and appears to, have a similar interaction domain. Our analysis demonstrates that TvFd has, a unique cavity near the iron-sulfur cluster that exposes one of the, inorganic sulfur atoms of the cluster to solvent. This cavity is not seen, in any other [2Fe-2S] ferredoxin with known structure, and is hypothesized, to be responsible for the high rate of metronidazole reduction by TvFd.
<StructureSection load='1l5p' size='340' side='right'caption='[[1l5p]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1l5p]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L5P 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]] 2.2&#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=1l5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5p OCA], [https://pdbe.org/1l5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l5p RCSB], [https://www.ebi.ac.uk/pdbsum/1l5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l5p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER_TRIVA FER_TRIVA] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. It links pyruvate:ferredoxin oxidoreductase to hydrogenase.
== 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/l5/1l5p_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=1l5p ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Crystallographic studies revealing the three-dimensional structure of the oxidized form of the [2Fe-2S] ferredoxin from Trichomonas vaginalis (TvFd) are presented. TvFd, a member of the hydrogenosomal class of ferredoxins, possesses a unique combination of redox and spectroscopic properties, and is believed to be the biological molecule that activates the drug metronidazole reductively in the treatment of trichomoniasis. It is the first hydrogenosomal ferredoxin to have its structure determined. The structure of TvFd reveals a monomeric, 93 residue protein with a fold similar to that of other known [2Fe-2S] ferredoxins. It contains nine hydrogen bonds to the sulfur atoms of the cluster, which is more than the number predicted on the basis of the spectroscopic data. The TvFd structure contains a large dipole moment like adrenodoxin, and appears to have a similar interaction domain. Our analysis demonstrates that TvFd has a unique cavity near the iron-sulfur cluster that exposes one of the inorganic sulfur atoms of the cluster to solvent. This cavity is not seen in any other [2Fe-2S] ferredoxin with known structure, and is hypothesized to be responsible for the high rate of metronidazole reduction by TvFd.


==About this Structure==
The crystal structure of Trichomonas vaginalis ferredoxin provides insight into metronidazole activation.,Crossnoe CR, Germanas JP, LeMagueres P, Mustata G, Krause KL J Mol Biol. 2002 Apr 26;318(2):503-18. PMID:12051855<ref>PMID:12051855</ref>
1L5P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis] 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=1L5P OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The crystal structure of Trichomonas vaginalis ferredoxin provides insight into metronidazole activation., Crossnoe CR, Germanas JP, LeMagueres P, Mustata G, Krause KL, J Mol Biol. 2002 Apr 26;318(2):503-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12051855 12051855]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1l5p" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trichomonas vaginalis]]
[[Category: Trichomonas vaginalis]]
[[Category: Crossnoe, C.R.]]
[[Category: Crossnoe CR]]
[[Category: Germanas, J.P.]]
[[Category: Germanas JP]]
[[Category: Krause, K.L.]]
[[Category: Krause KL]]
[[Category: Magueres, P.Le.]]
[[Category: Le Magueres P]]
[[Category: Mustata, G.]]
[[Category: Mustata G]]
[[Category: FES]]
[[Category: [2fe-2s] cluster]]
[[Category: electron transfer]]
[[Category: iron-sulfur protein]]
[[Category: metalloprotein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:17:29 2007''
Retrieved from "https://proteopedia.org/1l5p"