1u00: Difference between revisions

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[[Image:1u00.jpg|left|200px]]


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==HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC==
The line below this paragraph, containing "STRUCTURE_1u00", creates the "Structure Box" on the page.
<StructureSection load='1u00' size='340' side='right'caption='[[1u00]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1u00]] is a 2 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=1U00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U00 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#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=1u00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u00 OCA], [https://pdbe.org/1u00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u00 RCSB], [https://www.ebi.ac.uk/pdbsum/1u00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u00 ProSAT]</span></td></tr>
{{STRUCTURE_1u00|  PDB=1u00  |  SCENE= }}
</table>
 
== Function ==
'''HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC'''
[https://www.uniprot.org/uniprot/HSCA_ECOLI HSCA_ECOLI] Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU.[HAMAP-Rule:MF_00679]
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
HscA, a specialized bacterial Hsp70-class molecular chaperone, interacts with the iron-sulfur cluster assembly protein IscU by recognizing a conserved LPPVK sequence motif. We report the crystal structure of the substrate-binding domain of HscA (SBD, residues 389-616) from Escherichia coli bound to an IscU-derived peptide, ELPPVKIHC. The crystals belong to the space group I222 and contain a single molecule in the asymmetric unit. Molecular replacement with the E.coli DnaK(SBD) model was used for phasing, and the HscA(SBD)-peptide model was refined to Rfactor=17.4% (Rfree=21.0%) at 1.95 A resolution. The overall structure of HscA(SBD) is similar to that of DnaK(SBD), although the alpha-helical subdomain (residues 506-613) is shifted up to 10 A relative to the beta-sandwich subdomain (residues 389-498) when compared to DnaK(SBD). The ELPPVKIHC peptide is bound in an extended conformation in a hydrophobic cleft in the beta-subdomain, which appears to be solvent-accessible via a narrow passageway between the alpha and beta-subdomains. The bound peptide is positioned in the reverse orientation of that observed in the DnaK(SBD)-NRLLLTG peptide complex placing the N and C termini of the peptide on opposite sides of the HscA(SBD) relative to the DnaK(SBD) complex. Modeling of the peptide in the DnaK-like forward orientation suggests that differences in hydrogen bonding interactions in the binding cleft and electrostatic interactions involving surface residues near the cleft contribute to the observed directional preference.
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u0/1u00_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
1U00 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=1U00 OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</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=1u00 ConSurf].
Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC., Cupp-Vickery JR, Peterson JC, Ta DT, Vickery LE, J Mol Biol. 2004 Sep 24;342(4):1265-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15351650 15351650]
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cupp-Vickery, J R.]]
[[Category: Cupp-Vickery JR]]
[[Category: Peterson, J C.]]
[[Category: Peterson JC]]
[[Category: Ta, D T.]]
[[Category: Ta DT]]
[[Category: Vickery, L E.]]
[[Category: Vickery LE]]
[[Category: Dnak]]
[[Category: Hsc66]]
[[Category: Hsca]]
[[Category: Hsp70]]
[[Category: Iscu]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:34:36 2008''