1fpo

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[[Image:1fpo.jpg|left|200px]]
 
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==HSC20 (HSCB), A J-TYPE CO-CHAPERONE FROM E. COLI==
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The line below this paragraph, containing "STRUCTURE_1fpo", creates the "Structure Box" on the page.
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<StructureSection load='1fpo' size='340' side='right'caption='[[1fpo]], [[Resolution|resolution]] 1.80&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'>[[1fpo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#8491;</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=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>
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{{STRUCTURE_1fpo| PDB=1fpo | SCENE= }}
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</table>
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== Function ==
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'''HSC20 (HSCB), A J-TYPE CO-CHAPERONE FROM E. COLI'''
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpo_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1FPO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPO OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=1fpo ConSurf].
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11124030 11124030]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cupp-Vickery, J R.]]
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[[Category: Cupp-Vickery JR]]
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[[Category: Vickery, L E.]]
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[[Category: Vickery LE]]
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[[Category: Molecular chaperone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:37:01 2008''
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Current revision

HSC20 (HSCB), A J-TYPE CO-CHAPERONE FROM E. COLI

PDB ID 1fpo

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