1q5l: Difference between revisions

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-{{Seed}}
-[[Image:1q5l.png|left|200px]]
-<!--
+==NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG==
-The line below this paragraph, containing "STRUCTURE_1q5l", creates the "Structure Box" on the page.
+<StructureSection load='1q5l' size='340' side='right'caption='[[1q5l]]' 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'>[[1q5l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q5L 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">Solution NMR</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=1q5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q5l OCA], [https://pdbe.org/1q5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q5l RCSB], [https://www.ebi.ac.uk/pdbsum/1q5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q5l ProSAT]</span></td></tr>
-{{STRUCTURE_1q5l|  PDB=1q5l  |  SCENE=  }}
+</table>
+== Function ==
+[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]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q5/1q5l_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1q5l ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The Hsp70 family of molecular chaperones participates in a number of cellular processes, including binding to nascent polypeptide chains and assistance in protein (re)folding and degradation. We present the solution structure of the substrate binding domain (residues 393-507) of the Escherichia coli Hsp70, DnaK, that is bound to the peptide NRLLLTG and compare it to the crystal structure of DnaK(389-607) bound to the same peptide. The construct discussed here does not contain the alpha-helical domain that characterizes earlier published peptide-bound structures of the Hsp70s. It is established that removing the alpha-helical domain in its entirety does not affect the primary interactions or structure of the DnaK(393-507) in complex with the peptide NRLLLTG. In particular, the arch that protects the substrate-binding cleft is also formed in the absence of the helical lid. 15N-relaxation measurements show that the peptide-bound form of DnaK(393-507) is relatively rigid. As compared to the peptide-free state, the peptide-bound state of the domain shows distinct, widespread, and contiguous differences in structure extending toward areas previously defined as important to the allosteric regulation of the Hsp70 chaperones.
-===NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG===
+The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG.,Stevens SY, Cai S, Pellecchia M, Zuiderweg ER Protein Sci. 2003 Nov;12(11):2588-96. PMID:14573869<ref>PMID:14573869</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1q5l" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_14573869}}, adds the Publication Abstract to the page
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 14573869 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14573869}}
+__TOC__
+</StructureSection>
-==About this Structure==
-Q5L is a [[Single protein]] structure of 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=1Q5L OCA].
-==Reference==
-The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG., Stevens SY, Cai S, Pellecchia M, Zuiderweg ER, Protein Sci. 2003 Nov;12(11):2588-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14573869 14573869]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Homo sapiens]]
-[[Category: Cai, S.]]
+[[Category: Large Structures]]
-[[Category: Pellecchia, M.]]
+[[Category: Cai S]]
-[[Category: Stevens, S Y.]]
+[[Category: Pellecchia M]]
-[[Category: Zuiderweg, E R.]]
+[[Category: Stevens SY]]
-[[Category: Chaperone]]
+[[Category: Zuiderweg ER]]
-[[Category: Heat shock protein]]
-[[Category: Hsp70]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:35:51 2008''