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3bvo

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Revision as of 08:12, 25 October 2017

Crystal structure of human co-chaperone protein HscB

Structural highlights

3bvo is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Gene:	HSCB, DNAJC20, HSC20 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[HSC20_HUMAN] Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Uhrigshardt H, Singh A, Kovtunovych G, Ghosh M, Rouault TA. Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis. Hum Mol Genet. 2010 Oct 1;19(19):3816-34. doi: 10.1093/hmg/ddq301. Epub 2010 Jul , 28. PMID:20668094 doi:http://dx.doi.org/10.1093/hmg/ddq301
↑ Bitto E, Bingman CA, Bittova L, Kondrashov DA, Bannen RM, Fox BG, Markley JL, Phillips GN Jr. Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain. J Biol Chem. 2008 Oct 31;283(44):30184-92. Epub 2008 Aug 19. PMID:18713742 doi:10.1074/jbc.M804746200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bvo"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human co-chaperone protein HscB==
 <StructureSection load='3bvo' size='340' side='right' caption='[[3bvo]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bvo OCA], [http://pdbe.org/3bvo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bvo RCSB], [http://www.ebi.ac.uk/pdbsum/3bvo PDBsum], [http://www.topsan.org/Proteins/CESG/3bvo TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bvo OCA], [http://pdbe.org/3bvo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bvo RCSB], [http://www.ebi.ac.uk/pdbsum/3bvo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bvo ProSAT], [http://www.topsan.org/Proteins/CESG/3bvo TOPSAN]</span></td></tr>
 </table>
 == Function ==

3bvo

From Proteopedia

Revision as of 08:12, 25 October 2017

Crystal structure of human co-chaperone protein HscB

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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