3a39

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[[Image:3a39.png|left|200px]]
 
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{{STRUCTURE_3a39| PDB=3a39 | SCENE= }}
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==Crystal Structure of High-Potential Iron-Sulfur Protein from Thermochromatium tepidum at 0.72 angstrom resolution==
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<StructureSection load='3a39' size='340' side='right'caption='[[3a39]], [[Resolution|resolution]] 0.72&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3a39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermochromatium_tepidum Thermochromatium tepidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A39 FirstGlance]. <br>
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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]] 0.72&#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=GOL:GLYCEROL'>GOL</scene>, <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=3a39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a39 OCA], [https://pdbe.org/3a39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a39 RCSB], [https://www.ebi.ac.uk/pdbsum/3a39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a39 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HIP_THETI HIP_THETI] 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/a3/3a39_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=3a39 ConSurf].
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<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 positions of hydrogen atoms significantly define protein functions. However, such information from protein crystals is easily disturbed by X-rays. The damage can not be prevented completely even in the data collection at cryogenic temperatures. Therefore, the influence of X-rays should be precisely estimated in order to derive meaningful information from the crystallographic results. Diffraction data from a single crystal of the high-potential iron-sulfur protein (HiPIP) from Thermochromatium tepidum were collected at an undulator beamline of a third generation synchrotron facility, and were merged into three data sets according to X-ray dose. A series of structures analyzed at 0.70A shows detailed views of the X-ray induced perturbation, such as the positional changes of hydrogen atoms of a water molecule. Based on the results, we successfully collected a low perturbation data set using attenuated X-rays. There was no influence on the crystallographic statistics, such as the relative B factors, during the course of data collection. The electron densities for hydrogen atoms were more clear despite the slightly lower resolution.
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===Crystal Structure of High-Potential Iron-Sulfur Protein from Thermochromatium tepidum at 0.72 angstrom resolution===
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Detailed assessment of X-ray induced structural perturbation in a crystalline state protein.,Takeda K, Kusumoto K, Hirano Y, Miki K J Struct Biol. 2010 Feb;169(2):135-44. Epub 2009 Sep 24. PMID:19782139<ref>PMID:19782139</ref>
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{{ABSTRACT_PUBMED_19782139}}
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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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==About this Structure==
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<div class="pdbe-citations 3a39" style="background-color:#fffaf0;"></div>
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[[3a39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermochromatium_tepidum Thermochromatium tepidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A39 OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:019782139</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermochromatium tepidum]]
[[Category: Thermochromatium tepidum]]
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[[Category: Hirano, Y.]]
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[[Category: Hirano Y]]
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[[Category: Kusumoto, K.]]
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[[Category: Kusumoto K]]
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[[Category: Miki, K.]]
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[[Category: Miki K]]
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[[Category: Takeda, K.]]
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[[Category: Takeda K]]
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[[Category: Electron transport]]
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[[Category: Iron-sulfur cluster]]
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Current revision

Crystal Structure of High-Potential Iron-Sulfur Protein from Thermochromatium tepidum at 0.72 angstrom resolution

PDB ID 3a39

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