4f00 - Revision history

OCA at 11:07, 1 March 2024

2024-03-01T11:07:23Z

←Older revision		Revision as of 11:07, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4f00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombus_pascuorum Bombus pascuorum] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F00 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4f00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombus_pascuorum Bombus pascuorum] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F00 FirstGlance]. <br>
-	</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=4f00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f00 OCA], [https://pdbe.org/4f00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f00 RCSB], [https://www.ebi.ac.uk/pdbsum/4f00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f00 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.95Å</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=4f00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f00 OCA], [https://pdbe.org/4f00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f00 RCSB], [https://www.ebi.ac.uk/pdbsum/4f00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f00 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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]		[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]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Hsp70 chaperones have been implicated in assisting protein folding of newly synthesized polypeptide chains, refolding of misfolded proteins, and protein trafficking. For these functions, the chaperones need to exhibit a significant promiscuity in binding to different sequences of hydrophobic peptide stretches. To characterize the structural basis of sequence specificity and flexibility of the Escherichia coli Hsp70 chaperone DnaK, we have analyzed crystal structures of the substrate binding domain of the protein in complex with artificially designed peptides as well as small proline-rich antimicrobial peptides. Proline-rich antimicrobial peptides from mammals and insects were identified to target DnaK after cell penetration. Interestingly, the complex crystal structures reveal two different peptide binding modes. The peptides can bind either in a forward or in a reverse direction to the conventional substrate binding cleft of DnaK in an extended conformation. Superposition of the two binding modes shows a remarkable similarity in the side-chain orientations and hydrogen-bonding pattern despite the reversed peptide orientation. The DnaK chaperone has evolved to bind peptides in both orientations in the substrate binding cleft with comparable energy without rearrangements of the protein. Optimal hydrophobic interactions with binding pockets -2 to 0 appear to be the main determinant for the orientation and sequence position of peptide binding.
-
-	Structural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK.,Zahn M, Berthold N, Kieslich B, Knappe D, Hoffmann R, Strater N J Mol Biol. 2013 Apr 2. pii: S0022-2836(13)00208-8. doi:, 10.1016/j.jmb.2013.03.041. PMID:23562829<ref>PMID:23562829</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4f00" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]		*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 04:25, 7 October 2022

2022-10-07T04:25:12Z

←Older revision		Revision as of 04:25, 7 October 2022
Line 1:		Line 1:

	==Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)==		==Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)==
-	<StructureSection load='4f00' size='340' side='right' caption='[[4f00]], [[Resolution\|resolution]] 1.95Å' scene=''>	+	<StructureSection load='4f00' size='340' side='right'caption='[[4f00]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4f00]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4F00 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4f00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombus_pascuorum Bombus pascuorum] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F00 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dkx\|1dkx]], [[1dky\|1dky]], [[1dkz\|1dkz]], [[3dpo\|3dpo]], [[3dpp\|3dpp]], [[3dpq\|3dpq]], [[3qnj\|3qnj]], [[4e81\|4e81]], [[4ezn\|4ezn]], [[4ezo\|4ezo]], [[4ezp\|4ezp]], [[4ezq\|4ezq]], [[4ezr\|4ezr]], [[4ezs\|4ezs]], [[4ezt\|4ezt]], [[4ezu\|4ezu]], [[4ezv\|4ezv]], [[4ezw\|4ezw]], [[4ezx\|4ezx]], [[4ezy\|4ezy]], [[4ezz\|4ezz]], [[4f01\|4f01]]</td></tr>	+	</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=4f00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f00 OCA], [https://pdbe.org/4f00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f00 RCSB], [https://www.ebi.ac.uk/pdbsum/4f00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f00 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0014, dnaK, groP, grpF, JW0013, seg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4f00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f00 OCA], [~~http~~://pdbe.org/4f00 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4f00 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4f00 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4f00 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://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] ~~[[http://www.uniprot.org/uniprot/APID_BOMPA APID_BOMPA]] Antibacterial peptide active against Gram-negative bacteria.~~	+	[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]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 4f00" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4f00" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Bombus pascuorum]]
-	[[Category: ~~Straeter, N~~]]	+	[[Category: Escherichia coli K-12]]
-	[[Category: ~~Zahn, M~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Chaperone~~]]	+	[[Category: Straeter N]]
-	[[Category: ~~Chaperone-immune system complex]]~~	+	[[Category: Zahn M]]
-	~~[[Category: Peptide binding mode~~]]	+

OCA at 08:12, 15 November 2017

2017-11-15T08:12:31Z

←Older revision		Revision as of 08:12, 15 November 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4f00" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4f00" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Heat Shock Proteins\|Heat Shock Proteins]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:40, 5 August 2016

2016-08-05T18:40:24Z

←Older revision		Revision as of 18:40, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)==		==Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)==
	<StructureSection load='4f00' size='340' side='right' caption='[[4f00]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='4f00' size='340' side='right' caption='[[4f00]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4f00]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli_k-12 Escherichia coli k-12~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F00 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4f00]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F00 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dkx\|1dkx]], [[1dky\|1dky]], [[1dkz\|1dkz]], [[3dpo\|3dpo]], [[3dpp\|3dpp]], [[3dpq\|3dpq]], [[3qnj\|3qnj]], [[4e81\|4e81]], [[4ezn\|4ezn]], [[4ezo\|4ezo]], [[4ezp\|4ezp]], [[4ezq\|4ezq]], [[4ezr\|4ezr]], [[4ezs\|4ezs]], [[4ezt\|4ezt]], [[4ezu\|4ezu]], [[4ezv\|4ezv]], [[4ezw\|4ezw]], [[4ezx\|4ezx]], [[4ezy\|4ezy]], [[4ezz\|4ezz]], [[4f01\|4f01]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dkx\|1dkx]], [[1dky\|1dky]], [[1dkz\|1dkz]], [[3dpo\|3dpo]], [[3dpp\|3dpp]], [[3dpq\|3dpq]], [[3qnj\|3qnj]], [[4e81\|4e81]], [[4ezn\|4ezn]], [[4ezo\|4ezo]], [[4ezp\|4ezp]], [[4ezq\|4ezq]], [[4ezr\|4ezr]], [[4ezs\|4ezs]], [[4ezt\|4ezt]], [[4ezu\|4ezu]], [[4ezv\|4ezv]], [[4ezw\|4ezw]], [[4ezx\|4ezx]], [[4ezy\|4ezy]], [[4ezz\|4ezz]], [[4f01\|4f01]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0014, dnaK, groP, grpF, JW0013, seg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ~~Escherichia coli K-12~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0014, dnaK, groP, grpF, JW0013, seg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f00 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f00 RCSB], [http://www.ebi.ac.uk/pdbsum/4f00 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f00 OCA], [http://pdbe.org/4f00 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f00 RCSB], [http://www.ebi.ac.uk/pdbsum/4f00 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f00 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4f00" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Heat Shock Proteins\|Heat Shock Proteins]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli k-12~~]]	+	[[Category: Ecoli]]
	[[Category: Straeter, N]]		[[Category: Straeter, N]]
	[[Category: Zahn, M]]		[[Category: Zahn, M]]

OCA at 04:54, 25 December 2014

2014-12-25T04:54:07Z

←Older revision		Revision as of 04:54, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4f00\| PDB=4f00 \| SCENE= }}~~	+	==Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)==
-	===Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)===	+	<StructureSection load='4f00' size='340' side='right' caption='[[4f00]], [[Resolution\|resolution]] 1.95Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23562829}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4f00]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F00 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dkx\|1dkx]], [[1dky\|1dky]], [[1dkz\|1dkz]], [[3dpo\|3dpo]], [[3dpp\|3dpp]], [[3dpq\|3dpq]], [[3qnj\|3qnj]], [[4e81\|4e81]], [[4ezn\|4ezn]], [[4ezo\|4ezo]], [[4ezp\|4ezp]], [[4ezq\|4ezq]], [[4ezr\|4ezr]], [[4ezs\|4ezs]], [[4ezt\|4ezt]], [[4ezu\|4ezu]], [[4ezv\|4ezv]], [[4ezw\|4ezw]], [[4ezx\|4ezx]], [[4ezy\|4ezy]], [[4ezz\|4ezz]], [[4f01\|4f01]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0014, dnaK, groP, grpF, JW0013, seg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f00 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f00 RCSB], [http://www.ebi.ac.uk/pdbsum/4f00 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://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] [[http://www.uniprot.org/uniprot/APID_BOMPA APID_BOMPA]] Antibacterial peptide active against Gram-negative bacteria.		[[http://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] [[http://www.uniprot.org/uniprot/APID_BOMPA APID_BOMPA]] Antibacterial peptide active against Gram-negative bacteria.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Hsp70 chaperones have been implicated in assisting protein folding of newly synthesized polypeptide chains, refolding of misfolded proteins, and protein trafficking. For these functions, the chaperones need to exhibit a significant promiscuity in binding to different sequences of hydrophobic peptide stretches. To characterize the structural basis of sequence specificity and flexibility of the Escherichia coli Hsp70 chaperone DnaK, we have analyzed crystal structures of the substrate binding domain of the protein in complex with artificially designed peptides as well as small proline-rich antimicrobial peptides. Proline-rich antimicrobial peptides from mammals and insects were identified to target DnaK after cell penetration. Interestingly, the complex crystal structures reveal two different peptide binding modes. The peptides can bind either in a forward or in a reverse direction to the conventional substrate binding cleft of DnaK in an extended conformation. Superposition of the two binding modes shows a remarkable similarity in the side-chain orientations and hydrogen-bonding pattern despite the reversed peptide orientation. The DnaK chaperone has evolved to bind peptides in both orientations in the substrate binding cleft with comparable energy without rearrangements of the protein. Optimal hydrophobic interactions with binding pockets -2 to 0 appear to be the main determinant for the orientation and sequence position of peptide binding.

-	~~==About this Structure==~~	+	Structural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK.,Zahn M, Berthold N, Kieslich B, Knappe D, Hoffmann R, Strater N J Mol Biol. 2013 Apr 2. pii: S0022-2836(13)00208-8. doi:, 10.1016/j.jmb.2013.03.041. PMID:23562829<ref>PMID:23562829</ref>
-	~~[[4f00]] is a~~ 2 ~~chain structure with sequence from [http~~:~~//en.wikipedia.org/wiki/Escherichia_coli_k~~-~~12 Escherichia coli k~~-~~12]~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=4F00 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:023562829</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
-	[[Category: Straeter, N.]]	+	[[Category: Straeter, N]]
-	[[Category: Zahn, M.]]	+	[[Category: Zahn, M]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Chaperone-immune system complex]]		[[Category: Chaperone-immune system complex]]
	[[Category: Peptide binding mode]]		[[Category: Peptide binding mode]]

OCA at 04:34, 18 July 2013

2013-07-18T04:34:00Z

←Older revision		Revision as of 04:34, 18 July 2013
Line 8:		Line 8:
	==About this Structure==		==About this Structure==
	[[4f00]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA].		[[4f00]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:023562829</ref><references group="xtra"/><references/>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
	[[Category: Straeter, N.]]		[[Category: Straeter, N.]]

OCA at 20:25, 17 April 2013

2013-04-17T20:25:36Z

←Older revision		Revision as of 20:25, 17 April 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4f00\| PDB=4f00 \| SCENE= }}
		+	===Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)===
		+	{{ABSTRACT_PUBMED_23562829}}

-	~~The entry 4f00~~ is ~~ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://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] [[http://www.uniprot.org/uniprot/APID_BOMPA APID_BOMPA]] Antibacterial peptide active against Gram-negative bacteria.

-	~~Authors~~: ~~Zahn, M~~., Straeter, N.	+	==About this Structure==
-		+	[[4f00]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F00 OCA].
-	~~Description~~: ~~Crystal structure of the substrate binding domain of E~~.~~coli DnaK in~~ complex ~~with an apidaecin fragment from the bumblebee (residues 3 to 11)~~	+	[[Category: Escherichia coli k-12]]
		+	[[Category: Straeter, N.]]
		+	[[Category: Zahn, M.]]
		+	[[Category: Chaperone]]
		+	[[Category: Chaperone-immune system complex]]
		+	[[Category: Peptide binding mode]]

OCA at 05:17, 15 August 2012

2012-08-15T05:17:10Z

←Older revision		Revision as of 05:17, 15 August 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4f00 is ON HOLD	+	The entry 4f00 is ON HOLD until Paper Publication

	Authors: Zahn, M., Straeter, N.		Authors: Zahn, M., Straeter, N.

	Description: Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)		Description: Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)

OCA: Protected "4f00" [edit=sysop:move=sysop]

2012-05-09T08:55:50Z

Protected "4f00" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:55, 9 May 2012

OCA: New page: '''Unreleased structure''' The entry 4f00 is ON HOLD Authors: Zahn, M., Straeter, N. Description: Crystal structure of the substrate binding domain of E.coli DnaK in complex with an ap...

2012-05-09T08:55:50Z

New page: '''Unreleased structure''' The entry 4f00 is ON HOLD Authors: Zahn, M., Straeter, N. Description: Crystal structure of the substrate binding domain of E.coli DnaK in complex with an ap...

New page

'''Unreleased structure'''

The entry 4f00 is ON HOLD

Authors: Zahn, M., Straeter, N.

Description: Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11)