1bpr: Difference between revisions

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-{{Seed}}
-[[Image:1bpr.png|left|200px]]
-<!--
+==NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE==
-The line below this paragraph, containing "STRUCTURE_1bpr", creates the "Structure Box" on the page.
+<StructureSection load='1bpr' size='340' side='right'caption='[[1bpr]]' 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'>[[1bpr]] 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=1BPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BPR 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=1bpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bpr OCA], [https://pdbe.org/1bpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bpr RCSB], [https://www.ebi.ac.uk/pdbsum/1bpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bpr ProSAT]</span></td></tr>
-{{STRUCTURE_1bpr|  PDB=1bpr  |  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/bp/1bpr_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=1bpr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The solution structure of the 21 kDa substrate-binding domain of the Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to a precision of 1.00 A (backbone of the beta-domain) from 1075 experimental restraints obtained from multinuclear, multidimensional NMR experiments. The domain is observed to bind to its own C-terminus and offers a preview of the interaction of this chaperone with other proteins. The bound protein region is tightly held at a single amino acid position (a leucyl residue) that is buried in a deep pocket lined with conserved hydrophobic residues. A second hydrophobic binding site was identified using paramagnetically labeled peptides. It is located in a region close to the N-terminus of the domain and may constitute the allosteric region that links substrate-binding affinity with nucleotide binding in the Hsp70 chaperones.
-===NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE===
+NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.,Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER Biochemistry. 1998 Jun 2;37(22):7929-40. PMID:9609686<ref>PMID:9609686</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1bpr" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9609686}}, 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 9609686 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9609686}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BPR is a 1 chain 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=1BPR OCA].
-==Reference==
-<ref group="xtra">PMID:9609686</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Flynn, G C.]]
+[[Category: Large Structures]]
-[[Category: Hu, W.]]
+[[Category: Flynn GC]]
-[[Category: Kurochkin, A V.]]
+[[Category: Hu W]]
-[[Category: Pang, Y.]]
+[[Category: Kurochkin AV]]
-[[Category: Wang, H.]]
+[[Category: Pang Y]]
-[[Category: Zuiderweg, E R.P.]]
+[[Category: Wang H]]
-[[Category: Hsp70]]
+[[Category: Zuiderweg ERP]]
-[[Category: Molecular chaperone]]
-[[Category: Peptide binding]]
-[[Category: Protein folding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:11:51 2009''