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1pc4

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[[Image:1pc4.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of the P50A mutant of ferredoxin I at 1.65 A Resolution==
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|PDB= 1pc4 |SIZE=350|CAPTION= <scene name='initialview01'>1pc4</scene>, resolution 1.65&Aring;
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<StructureSection load='1pc4' size='340' side='right'caption='[[1pc4]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=F3S:FE3-S4 CLUSTER'>F3S</scene>
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<table><tr><td colspan='2'>[[1pc4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PC4 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pc4 OCA], [https://pdbe.org/1pc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pc4 RCSB], [https://www.ebi.ac.uk/pdbsum/1pc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pc4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FER1_AZOVI FER1_AZOVI] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. This ferredoxin could play a role in regulating gene expression by interacting directly with DNA.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/1pc4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1pc4 ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of the P50A mutant of ferredoxin I at 1.65 A Resolution'''
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==See Also==
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The 7Fe ferredoxin from Azotobacter vinelandii (AvFdI) contains a [3Fe-4S](+/0) cluster that binds a single proton in its reduced level. Although the cluster is buried, and therefore inaccessible to solvent, proton transfer from solvent to the cluster is fast. The kinetics and energetics of the coupled electron-proton transfer reaction at the cluster have been analyzed in detail by protein-film voltammetry, to reveal that proton transfer is mediated by the mobile carboxylate of an adjacent surface residue, aspartate-15, the pK of which is sensitive to the charge on the cluster. This paper examines the role of a nearby proline residue, proline-50, in proton transfer and its coupling to electron transfer. In the P50A and P50G mutants, a water molecule has entered the cluster binding region; it is hydrogen bonded to the backbone amide of residue-50 and to the Asp-15 carboxylate, and it is approximately 4 A from the closest sulfur atom of the cluster. Despite the water molecule linking the cluster more directly to the solvent, proton transfer is not accelerated. A detailed analysis reveals that Asp-15 remains a central part of the mechanism. However, the electrostatic coupling between cluster and carboxylate is almost completely quenched, so that cluster reduction no longer induces such a favorable shift in the carboxylate pK, and protonation of the base no longer induces a significant shift in the pK of the cluster. The electrostatic coupling is crucial for maintaining the efficiency of proton transfer both to and from the cluster, over a range of pH values.
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==About this Structure==
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1PC4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC4 OCA].
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==Reference==
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Mechanisms of redox-coupled proton transfer in proteins: role of the proximal proline in reactions of the [3Fe-4S] cluster in Azotobacter vinelandii ferredoxin I., Camba R, Jung YS, Hunsicker-Wang LM, Burgess BK, Stout CD, Hirst J, Armstrong FA, Biochemistry. 2003 Sep 16;42(36):10589-99. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12962482 12962482]
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[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Armstrong, F A.]]
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[[Category: Armstrong FA]]
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[[Category: Burgess, B K.]]
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[[Category: Burgess BK]]
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[[Category: Camba, R.]]
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[[Category: Camba R]]
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[[Category: Chen, K.]]
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[[Category: Chen K]]
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[[Category: Hirst, J.]]
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[[Category: Hirst J]]
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[[Category: Hunsicker-Wang, L M.]]
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[[Category: Hunsicker-Wang LM]]
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[[Category: Jung, Y S.]]
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[[Category: Jung YS]]
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[[Category: Stout, C D.]]
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[[Category: Stout CD]]
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[[Category: F3S]]
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[[Category: SF4]]
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[[Category: electron transport]]
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[[Category: ferredoxin]]
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[[Category: iron-sulfur protein]]
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[[Category: mutant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:30 2008''
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Current revision

Crystal Structure of the P50A mutant of ferredoxin I at 1.65 A Resolution

PDB ID 1pc4

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