1hpi

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(New page: 200px<br /><applet load="1hpi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hpi, resolution 1.8&Aring;" /> '''MOLECULAR STRUCTURE O...)
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[[Image:1hpi.gif|left|200px]]<br /><applet load="1hpi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hpi, resolution 1.8&Aring;" />
 
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'''MOLECULAR STRUCTURE OF THE OXIDIZED HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA VACUOLATA'''<br />
 
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==Overview==
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==MOLECULAR STRUCTURE OF THE OXIDIZED HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA VACUOLATA==
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The high-potential iron-sulfur protein (iso-form II) isolated from, Ectothiorhodospira vacuolata has been crystallized and its, three-dimensional structure determined by molecular replacement procedures, and refined to 1.8-A resolution with a crystallographic R factor of 16.3%., Crystals employed in the investigation belonged to the space group C222(1), with unit cell dimensions of a = 58.4 A, b = 64.7 A, and c = 39.3 A and, one molecule per asymmetric unit. Like those HiPIPs structurally, characterized thus far, the E. vacuolata molecule contains mostly reverse, turns that wrap around the iron-sulfur cluster with cysteine residues 34, 37, 51, and 65 ligating the metal center to the polypeptide chain. There, are 57 ordered solvent molecules, most of which lie at the surface of the, protein. Two of these water molecules play important structural roles by, stabilizing the loops located between Asp 42 and Lys 57. The metal center, binding pocket is decidedly hydrophobic with the closest solvent molecule, being 6.9 A from S2 of the [4Fe-4S] cluster. The E. vacuolata HiPIP, molecules pack in the crystalline lattice as dimers with their iron-sulfur, centers approximately 17.5 A apart. On the basis of biochemical, properties, it was anticipated that the E. vacuolata HiPIP would be, structurally more similar to the HiPIP isolated from Ectothiorhodospira, halophila than to the protein obtained from Chromatium vinosum. In fact, the E. vacuolata molecule is as structurally close to the C. vinosum HiPIP, as it is to the E. halophila protein due to the presence of various, insertions and deletions that disrupt local folding.(ABSTRACT TRUNCATED AT, 250 WORDS)
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<StructureSection load='1hpi' size='340' side='right'caption='[[1hpi]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1hpi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ectothiorhodospira_shaposhnikovii Ectothiorhodospira shaposhnikovii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HPI FirstGlance]. <br>
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1HPI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ectothiorhodospira_shaposhnikovii Ectothiorhodospira shaposhnikovii] 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=1HPI OCA].
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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]] 1.8&#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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
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==Reference==
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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=1hpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hpi OCA], [https://pdbe.org/1hpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hpi RCSB], [https://www.ebi.ac.uk/pdbsum/1hpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hpi ProSAT]</span></td></tr>
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Molecular structure of the oxidized high-potential iron-sulfur protein isolated from Ectothiorhodospira vacuolata., Benning MM, Meyer TE, Rayment I, Holden HM, Biochemistry. 1994 Mar 8;33(9):2476-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8117708 8117708]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HIP2_ECTSH HIP2_ECTSH] 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.
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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/hp/1hpi_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=1hpi ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Ectothiorhodospira shaposhnikovii]]
[[Category: Ectothiorhodospira shaposhnikovii]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Benning, M.M.]]
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[[Category: Benning MM]]
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[[Category: Holden, H.M.]]
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[[Category: Holden HM]]
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[[Category: Meyer, T.E.]]
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[[Category: Meyer TE]]
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[[Category: Rayment, I.]]
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[[Category: Rayment I]]
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[[Category: SF4]]
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[[Category: electron transfer(iron-sulfur protein)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:43:38 2007''
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Current revision

MOLECULAR STRUCTURE OF THE OXIDIZED HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA VACUOLATA

PDB ID 1hpi

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