1hlq

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==CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A==
==CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A==
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<StructureSection load='1hlq' size='340' side='right' caption='[[1hlq]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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<StructureSection load='1hlq' size='340' side='right'caption='[[1hlq]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1hlq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodoferax_fermentans Rhodoferax fermentans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HLQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1hlq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodoferax_fermentans Rhodoferax fermentans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HLQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 1.45&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlq OCA], [http://pdbe.org/1hlq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hlq RCSB], [http://www.ebi.ac.uk/pdbsum/1hlq PDBsum]</span></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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1hlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlq OCA], [https://pdbe.org/1hlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hlq RCSB], [https://www.ebi.ac.uk/pdbsum/1hlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hlq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HIP_RHOFE HIP_RHOFE]] Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. Competent in photosynthetic electron transfer to oxidized cytochrome bc1 complex via the membrane-bound c-type tetraheme.<ref>PMID:7574702</ref> [:]<ref>PMID:8001683</ref> <ref>PMID:7498498</ref> <ref>PMID:8692932</ref> <ref>PMID:10076014</ref>
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[https://www.uniprot.org/uniprot/HIP_RHOFE HIP_RHOFE] Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. Competent in photosynthetic electron transfer to oxidized cytochrome bc1 complex via the membrane-bound c-type tetraheme.<ref>PMID:7574702</ref> [:]<ref>PMID:8001683</ref> <ref>PMID:7498498</ref> <ref>PMID:8692932</ref> <ref>PMID:10076014</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/1hlq_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/1hlq_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=1hlq ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The crystal structure of Rhodoferax fermentans high-potential iron protein (HiPIP) has been solved by MAD methods using the anomalous signal from the Fe atoms in the [Fe(4)S(4)] cluster present in the protein and refined to a resolution of 1.45 A. The peptide chain is well defined except in the N- and C-terminal areas. The structure of the protein reveals the presence of three helical fragments, a small beta-sheet and several turns, with the [Fe(4)S(4)] cluster being located close to a surface patch containing several well conserved aromatic residues. The protein fold is very similar to the structures of other known HiPIPs, especially in the region proximal to the [Fe(4)S(4)] cluster, while the largest differences are observed on the opposite side of the protein, which is rich in positive charges and has no sequential homology to other HiPIP families.
 
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Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD.,Gonzalez A, Benini S, Ciurli S Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1582-8. Epub 2003, Aug 19. PMID:12925788<ref>PMID:12925788</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1hlq" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Rhodoferax fermentans]]
[[Category: Rhodoferax fermentans]]
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[[Category: Benini, S]]
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[[Category: Benini S]]
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[[Category: Ciurli, S]]
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[[Category: Ciurli S]]
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[[Category: Gonzalez, A]]
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[[Category: Gonzalez A]]
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[[Category: Electron transport]]
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[[Category: Iron sulfur cluster]]
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Current revision

CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A

PDB ID 1hlq

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