1l5p: Difference between revisions

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{{Seed}}
[[Image:1l5p.png|left|200px]]


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==Crystal Structure of Trichomonas vaginalis Ferredoxin==
The line below this paragraph, containing "STRUCTURE_1l5p", creates the "Structure Box" on the page.
<StructureSection load='1l5p' size='340' side='right'caption='[[1l5p]], [[Resolution|resolution]] 2.20&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'>[[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>
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]] 2.2&#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></td></tr>
{{STRUCTURE_1l5p|  PDB=1l5p  |  SCENE=  }}
<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.


===Crystal Structure of Trichomonas vaginalis Ferredoxin===
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1l5p" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12051855}}, adds the Publication Abstract to the page
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12051855 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12051855}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1L5P is a 3 chains structure of sequences from [http://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].
 
==Reference==
<ref group="xtra">PMID:12051855</ref><references group="xtra"/>
[[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: Electron transfer]]
[[Category: Iron-sulfur protein]]
[[Category: Metalloprotein]]
 
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Retrieved from "https://proteopedia.org/1l5p"