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3bvo
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| - | [[Image:3bvo.jpg|left|200px]]<br /><applet load="3bvo" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="3bvo, resolution 3.000Å" /> | ||
| - | '''Crystal structure of human co-chaperone protein HscB'''<br /> | ||
| - | == | + | ==Crystal structure of human co-chaperone protein HscB== |
| - | + | <StructureSection load='3bvo' size='340' side='right'caption='[[3bvo]], [[Resolution|resolution]] 3.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3bvo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BVO FirstGlance]. <br> | |
| - | [ | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSCB, DNAJC20, HSC20 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |
| - | [[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bvo OCA], [https://pdbe.org/3bvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bvo RCSB], [https://www.ebi.ac.uk/pdbsum/3bvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bvo ProSAT], [https://www.topsan.org/Proteins/CESG/3bvo TOPSAN]</span></td></tr> |
| - | [[ | + | </table> |
| - | + | == Function == | |
| - | [ | + | [[https://www.uniprot.org/uniprot/HSC20_HUMAN HSC20_HUMAN]] Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria.<ref>PMID:20668094</ref> |
| - | [[ | + | == Evolutionary Conservation == |
| - | [ | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/3bvo_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
| - | + | <text>to colour the structure by Evolutionary Conservation</text> | |
| - | + | </jmolCheckbox> | |
| - | + | </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=3bvo ConSurf]. | |
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Iron-sulfur proteins play indispensable roles in a broad range of biochemical processes. The biogenesis of iron-sulfur proteins is a complex process that has become a subject of extensive research. The final step of iron-sulfur protein assembly involves transfer of an iron-sulfur cluster from a cluster-donor to a cluster-acceptor protein. This process is facilitated by a specialized chaperone system, which consists of a molecular chaperone from the Hsc70 family and a co-chaperone of the J-domain family. The 3.0 A crystal structure of a human mitochondrial J-type co-chaperone HscB revealed an L-shaped protein that resembles Escherichia coli HscB. The important difference between the two homologs is the presence of an auxiliary metal-binding domain at the N terminus of human HscB that coordinates a metal via the tetracysteine consensus motif CWXCX(9-13)FCXXCXXXQ. The domain is found in HscB homologs from animals and plants as well as in magnetotactic bacteria. The metal-binding site of the domain is structurally similar to that of rubredoxin and several zinc finger proteins containing rubredoxin-like knuckles. The normal mode analysis of HscB revealed that this L-shaped protein preferentially undergoes a scissors-like motion that correlates well with the conformational changes of human HscB observed in the crystals. | ||
| - | + | Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain.,Bitto E, Bingman CA, Bittova L, Kondrashov DA, Bannen RM, Fox BG, Markley JL, Phillips GN Jr J Biol Chem. 2008 Oct 31;283(44):30184-92. Epub 2008 Aug 19. PMID:18713742<ref>PMID:18713742</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3bvo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bingman, C A]] | ||
| + | [[Category: Bitto, E]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: McCoy, J G]] | ||
| + | [[Category: Phillips, G N]] | ||
| + | [[Category: Wesenberg, G E]] | ||
| + | [[Category: Cesg]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Co-chaperone protein hscb]] | ||
| + | [[Category: Mitochondrion]] | ||
| + | [[Category: PSI, Protein structure initiative]] | ||
| + | [[Category: Transit peptide]] | ||
Current revision
Crystal structure of human co-chaperone protein HscB
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