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3bvo

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{{Seed}}
 
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[[Image:3bvo.png|left|200px]]
 
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==Crystal structure of human co-chaperone protein HscB==
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The line below this paragraph, containing "STRUCTURE_3bvo", creates the "Structure Box" on the page.
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<StructureSection load='3bvo' size='340' side='right'caption='[[3bvo]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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-->
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<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>
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{{STRUCTURE_3bvo| PDB=3bvo | SCENE= }}
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<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>
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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=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>
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</table>
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== Function ==
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[[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>
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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/bv/3bvo_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=3bvo 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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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.
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===Crystal structure of human co-chaperone protein HscB===
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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>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_18713742}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3bvo" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18713742 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_18713742}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human]]
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3BVO is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BVO OCA].
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[[Category: Large Structures]]
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[[Category: Bingman, C A]]
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==Reference==
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[[Category: Bitto, E]]
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<ref group="xtra">PMID:18713742</ref><references group="xtra"/>
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[[Category: Structural genomic]]
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[[Category: Homo sapiens]]
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[[Category: McCoy, J G]]
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[[Category: Bingman, C A.]]
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[[Category: Phillips, G N]]
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[[Category: Bitto, E.]]
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[[Category: Wesenberg, G E]]
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[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
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[[Category: Jr., G N.Phillips.]]
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[[Category: McCoy, J G.]]
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[[Category: Wesenberg, G E.]]
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[[Category: Center for eukaryotic structural genomic]]
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[[Category: Cesg]]
[[Category: Cesg]]
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[[Category: Chaperone]]
[[Category: Co-chaperone protein hscb]]
[[Category: Co-chaperone protein hscb]]
[[Category: Mitochondrion]]
[[Category: Mitochondrion]]
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[[Category: Protein structure initiative]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Psi-2]]
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[[Category: Structural genomics medical relevance]]
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[[Category: Transit peptide]]
[[Category: Transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:16:32 2009''
 

Current revision

Crystal structure of human co-chaperone protein HscB

PDB ID 3bvo

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