2kho

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[[Image:2kho.png|left|200px]]
 
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==NMR-RDC / XRAY structure of E. coli HSP70 (DNAK) chaperone (1-605) complexed with ADP and substrate==
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The line below this paragraph, containing "STRUCTURE_2kho", creates the "Structure Box" on the page.
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<StructureSection load='2kho' size='340' side='right'caption='[[2kho]]' 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'>[[2kho]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KHO 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">Solution NMR</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=2kho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kho OCA], [https://pdbe.org/2kho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kho RCSB], [https://www.ebi.ac.uk/pdbsum/2kho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kho ProSAT]</span></td></tr>
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{{STRUCTURE_2kho| PDB=2kho | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DNAK_ECOLI DNAK_ECOLI] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332]
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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/kh/2kho_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=2kho 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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DnaK is the canonical Hsp70 molecular chaperone protein from Escherichia coli. Like other Hsp70s, DnaK comprises two main domains: a 44-kDa N-terminal nucleotide-binding domain (NBD) that contains ATPase activity, and a 25-kDa substrate-binding domain (SBD) that harbors the substrate-binding site. Here, we report an experimental structure for wild-type, full-length DnaK, complexed with the peptide NRLLLTG and with ADP. It was obtained in aqueous solution by using NMR residual dipolar coupling and spin labeling methods and is based on available crystal structures for the isolated NBD and SBD. By using dynamics methods, we determine that the NBD and SBD are loosely linked and can move in cones of +/-35 degrees with respect to each other. The linker region between the domains is a dynamic random coil. Nevertheless, an average structure can be defined. This structure places the SBD in close proximity of subdomain IA of the NBD and suggests that the SBD collides with the NBD at this area to establish allosteric communication.
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===NMR-RDC / XRAY structure of E. coli HSP70 (DNAK) chaperone (1-605) complexed with ADP and substrate===
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Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.,Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ER Proc Natl Acad Sci U S A. 2009 May 26;106(21):8471-6. Epub 2009 May 13. PMID:19439666<ref>PMID:19439666</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_19439666}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2kho" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19439666 is the PubMed ID number.
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{{ABSTRACT_PUBMED_19439666}}
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==About this Structure==
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[[2kho]] is a 1 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHO OCA].
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==See Also==
==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[Heat Shock Proteins|Heat Shock Proteins]]
*[[Heat Shock Proteins|Heat Shock Proteins]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:019439666</ref><references group="xtra"/>
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__TOC__
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[[Category: Escherichia coli]]
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</StructureSection>
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[[Category: Bertelsen, E B.]]
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[[Category: Escherichia coli K-12]]
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[[Category: Zuiderweg, E R.P.]]
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[[Category: Large Structures]]
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[[Category: Atp-binding]]
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[[Category: Bertelsen EB]]
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[[Category: Cell inner membrane]]
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[[Category: Zuiderweg ERP]]
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[[Category: Cell membrane]]
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[[Category: Chaperone]]
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[[Category: Dna replication]]
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[[Category: Hsp70]]
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[[Category: Membrane]]
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[[Category: Molecular chaperone]]
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[[Category: Nucleotide-binding]]
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[[Category: Peptide binding]]
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[[Category: Phosphoprotein]]
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[[Category: Protein folding]]
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[[Category: Stress response]]
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[[Category: Transcription]]
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Current revision

NMR-RDC / XRAY structure of E. coli HSP70 (DNAK) chaperone (1-605) complexed with ADP and substrate

PDB ID 2kho

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