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2hip

From Proteopedia

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[[Image:2hip.jpg|left|200px]]
 
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{{Structure
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==THE MOLECULAR STRUCTURE OF THE HIGH POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA HALOPHILA DETERMINED AT 2.5-ANGSTROMS RESOLUTION==
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|PDB= 2hip |SIZE=350|CAPTION= <scene name='initialview01'>2hip</scene>, resolution 2.5&Aring;
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<StructureSection load='2hip' size='340' side='right'caption='[[2hip]], [[Resolution|resolution]] 2.50&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>
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<table><tr><td colspan='2'>[[2hip]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HIP 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]] 2.5&#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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
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|DOMAIN=
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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=2hip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hip OCA], [https://pdbe.org/2hip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hip RCSB], [https://www.ebi.ac.uk/pdbsum/2hip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hip ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hip OCA], [http://www.ebi.ac.uk/pdbsum/2hip PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hip RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/HIP1_HALHA HIP1_HALHA] 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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'''THE MOLECULAR STRUCTURE OF THE HIGH POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA HALOPHILA DETERMINED AT 2.5-ANGSTROMS RESOLUTION'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hi/2hip_consurf.spt"</scriptWhenChecked>
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The molecular structure of a high potential iron-sulfur protein (HiPIP) isolated from the purple photosynthetic bacterium, Ectothiorhodospira halophila strain BN9626, has been solved by x-ray diffraction analysis to a nominal resolution of 2.5 A and refined to a crystallographic R value of 18.4% including all measured x-ray data from 30.0- to 2.5-A resolution. Crystals used in the investigation contained two molecules/asymmetric unit and belonged to the space group P21 with unit cell dimensions of a = 60.00 A, b = 31.94 A, c = 40.27 A, and beta = 100.5 degrees. An interpretable electron density map, obtained by combining x-ray data from one isomorphous heavy atom derivative with non-crystallographic symmetry averaging and solvent flattening, clearly showed that this high potential iron-sulfur protein contains 71 amino acid residues, rather than 70 as originally reported. As in other bacterial ferredoxins, the [4Fe-4S] cluster adopts a cubane-like conformation and is ligated to the protein via four cysteinyl sulfur ligands. The overall secondary structure of the E. halophila HiPIP is characterized by a series of Type I and Type II turns allowing the polypeptide chain to wrap around the [4Fe-4S] prosthetic group. The hydrogen bonding pattern around the cluster is nearly identical to that originally observed in the 85-amino acid residue Chromatium vinosum HiPIP and consequently, the 240 mV difference in redox potentials between these two proteins cannot be simply attributed to hydrogen bonding patterns alone.
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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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==About this Structure==
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</jmolCheckbox>
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2HIP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIP OCA].
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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=2hip ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution., Breiter DR, Meyer TE, Rayment I, Holden HM, J Biol Chem. 1991 Oct 5;266(28):18660-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1917989 1917989]
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</StructureSection>
[[Category: Halorhodospira halophila]]
[[Category: Halorhodospira halophila]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Breiter, D R.]]
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[[Category: Breiter DR]]
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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: electron transfer (iron-sulfur protein)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:31:00 2008''
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Current revision

THE MOLECULAR STRUCTURE OF THE HIGH POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA HALOPHILA DETERMINED AT 2.5-ANGSTROMS RESOLUTION

PDB ID 2hip

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