1dg4

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(New page: 200px<br /><applet load="1dg4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dg4" /> '''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAI...)
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[[Image:1dg4.jpg|left|200px]]<br /><applet load="1dg4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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'''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK IN THE APO FORM'''<br />
 
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==Overview==
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==NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK IN THE APO FORM==
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How substrate affinity is modulated by nucleotide binding remains a, fundamental, unanswered question in the study of 70 kDa heat shock protein, (Hsp70) molecular chaperones. We find here that the Escherichia coli, Hsp70, DnaK, lacking the entire alpha-helical domain, DnaK(1-507), retains, the ability to support lambda phage replication in vivo and to pass, information from the nucleotide binding domain to the substrate binding, domain, and vice versa, in vitro. We determined the NMR solution structure, of the corresponding substrate binding domain, DnaK(393-507), without, substrate, and assessed the impact of substrate binding. Without bound, substrate, loop L3,4 and strand beta3 are in significantly different, conformations than observed in previous structures of the bound DnaK, substrate binding domain, leading to occlusion of the substrate binding, site. Upon substrate binding, the beta-domain shifts towards the structure, seen in earlier X-ray and NMR structures. Taken together, our results, suggest that conformational changes in the beta-domain itself contribute, to the mechanism by which nucleotide binding modulates substrate binding, affinity.
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<StructureSection load='1dg4' size='340' side='right'caption='[[1dg4]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dg4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DG4 FirstGlance]. <br>
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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=1dg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dg4 OCA], [https://pdbe.org/1dg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dg4 RCSB], [https://www.ebi.ac.uk/pdbsum/1dg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dg4 ProSAT]</span></td></tr>
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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/dg/1dg4_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=1dg4 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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How substrate affinity is modulated by nucleotide binding remains a fundamental, unanswered question in the study of 70 kDa heat shock protein (Hsp70) molecular chaperones. We find here that the Escherichia coli Hsp70, DnaK, lacking the entire alpha-helical domain, DnaK(1-507), retains the ability to support lambda phage replication in vivo and to pass information from the nucleotide binding domain to the substrate binding domain, and vice versa, in vitro. We determined the NMR solution structure of the corresponding substrate binding domain, DnaK(393-507), without substrate, and assessed the impact of substrate binding. Without bound substrate, loop L3,4 and strand beta3 are in significantly different conformations than observed in previous structures of the bound DnaK substrate binding domain, leading to occlusion of the substrate binding site. Upon substrate binding, the beta-domain shifts towards the structure seen in earlier X-ray and NMR structures. Taken together, our results suggest that conformational changes in the beta-domain itself contribute to the mechanism by which nucleotide binding modulates substrate binding affinity.
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==About this Structure==
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Structural insights into substrate binding by the molecular chaperone DnaK.,Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER Nat Struct Biol. 2000 Apr;7(4):298-303. PMID:10742174<ref>PMID:10742174</ref>
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1DG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DG4 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural insights into substrate binding by the molecular chaperone DnaK., Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER, Nat Struct Biol. 2000 Apr;7(4):298-303. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10742174 10742174]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1dg4" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Feng, H.]]
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[[Category: Gierasch, L.M.]]
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[[Category: Kooi, C.W.Van.der.]]
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[[Category: Montgomery, D.L.]]
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[[Category: Pellecchia, M.]]
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[[Category: Stevens, S.Y.]]
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[[Category: Zuiderweg, E.R.P.]]
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[[Category: chaperone]]
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[[Category: dnak]]
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[[Category: substrate binding domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:15:55 2007''
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Feng H]]
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[[Category: Gierasch LM]]
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[[Category: Montgomery DL]]
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[[Category: Pellecchia M]]
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[[Category: Stevens SY]]
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[[Category: Van der Kooi CW]]
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[[Category: Zuiderweg ERP]]

Current revision

NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK IN THE APO FORM

PDB ID 1dg4

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