1fca: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1fca" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fca, resolution 1.8Å" /> '''STRUCTURE OF THE FERR...
 
No edit summary
 
(19 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1fca.jpg|left|200px]]<br /><applet load="1fca" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fca, resolution 1.8&Aring;" />
'''STRUCTURE OF THE FERREDOXIN FROM CLOSTRIDIUM ACIDURICI: MODEL AT 1.8 ANGSTROMS RESOLUTION'''<br />


==Overview==
==STRUCTURE OF THE FERREDOXIN FROM CLOSTRIDIUM ACIDURICI: MODEL AT 1.8 ANGSTROMS RESOLUTION==
Ferredoxins (Fd) are electron-carrier proteins, the active sites of which, are organized around clusters made of iron and inorganic sulfur. The Fd, from Clostridium acidurici is 55 amino acids long and contains two, [4Fe-4S] clusters. Crystals have been obtained in the space group, P4(3)2(1)2, a = b = 34.441 (5), c = 74.778 (9) A. The structure was solved, by molecular replacement using the Fd from Peptostreptcoccus, asaccharolyticus as a search model, these two ferredoxins having 37, residues in common. Refinement using molecular-dynamics techniques was, then initiated. Successive rounds of model building and refinement gave a, structure that includes 45 water molecules with R = 15%. At this stage, the electron-density map clearly revealed discrepancies in the position of, two amino acids in the published primary sequence. Refinement based on, these modifications led to R = 14.3% for 3921 reflections up to 1.8 A, resolution. The geometry of the two clusters has been found to be in good, agreement with that previously obtained at a lower resolution., Interactions of polypeptide chain with the [4Fe-4S] clusters, the cluster, geometry as well as the hydrogen bonds involving S, Sgamma, N and water, molecules are reported.
<StructureSection load='1fca' size='340' side='right'caption='[[1fca]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fca]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gottschalkia_acidurici Gottschalkia acidurici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FCA 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=1fca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fca OCA], [https://pdbe.org/1fca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fca RCSB], [https://www.ebi.ac.uk/pdbsum/1fca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fca ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER_GOTA9 FER_GOTA9] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.[UniProtKB:P50727]
== 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/fc/1fca_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=1fca ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FCA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_acidurici Clostridium acidurici] with SF4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FCA OCA].
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure of the ferredoxin from Clostridium acidurici: model at 1.8 A resolution., TranQui D, Jesior JC, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):155-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299316 15299316]
[[Category: Gottschalkia acidurici]]
[[Category: Clostridium acidurici]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Jesior JC]]
[[Category: Jesior, J.C.]]
[[Category: Tranqui D]]
[[Category: Tranqui, D.]]
[[Category: SF4]]
[[Category: electron transport (cytochrome)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:48:45 2007''

Latest revision as of 10:13, 7 February 2024

STRUCTURE OF THE FERREDOXIN FROM CLOSTRIDIUM ACIDURICI: MODEL AT 1.8 ANGSTROMS RESOLUTIONSTRUCTURE OF THE FERREDOXIN FROM CLOSTRIDIUM ACIDURICI: MODEL AT 1.8 ANGSTROMS RESOLUTION

Structural highlights

1fca is a 1 chain structure with sequence from Gottschalkia acidurici. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FER_GOTA9 Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.[UniProtKB:P50727]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1fca, resolution 1.80Å

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