1fpo

<table><tr><td colspan='2'>[[1fpo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FPO FirstGlance]. <br>

</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=1fpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpo OCA], [https://pdbe.org/1fpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fpo RCSB], [https://www.ebi.ac.uk/pdbsum/1fpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpo ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/HSCB_ECOLI HSCB_ECOLI]] Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA.

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== Publication Abstract from PubMed ==

Hsc20 is a 20 kDa J-protein that regulates the ATPase activity and peptide-binding specificity of Hsc66, an hsp70-class molecular chaperone. We report herein the crystal structure of Hsc20 from Escherichia coli determined to a resolution of 1.8 A using a combination of single isomorphous replacement (SIR) and multi-wavelength anomalous diffraction (MAD). The overall structure of Hsc20 consists of two distinct domains, an N-terminal J-domain containing residues 1-75 connected by a short loop to a C-terminal domain containing residues 84-171. The structure of the J-domain, involved in interactions with Hsc66, resembles the alpha-topology of J-domain fragments of Escherichia coli DnaJ and human Hdj1 previously determined by solution NMR methods. The C-terminal domain, implicated in binding and targeting proteins to Hsc66, consists of a three-helix bundle in which two helices comprise an anti-parallel coiled-coil. The two domains make contact through an extensive hydrophobic interface ( approximately 650 A(2)) suggesting that their relative orientations are fixed. Thus, Hsc20, in addition to its role in the regulation of the ATPase activity of Hsc66, may also function as a rigid scaffold to facilitate positioning of the protein substrates targeted to Hsc66.

Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli.,Cupp-Vickery JR, Vickery LE J Mol Biol. 2000 Dec 15;304(5):835-45. PMID:11124030<ref>PMID:11124030</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Cupp-Vickery, J R]]

[[Category: Vickery, L E]]

[[Category: Molecular chaperone]]