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==Crystal structure of the substrate binding domain of E.coli DnaK in complex with sheep Bac7(35-43)== | |||
<StructureSection load='4jwi' size='340' side='right' caption='[[4jwi]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jwi]] is a 4 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=4JWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JWI FirstGlance]. <br> | |||
==Function== | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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]], [[4jwc|4jwc]], [[4jwd|4jwd]], [[4jwe|4jwe]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaK, groP, grpF, 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=4jwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jwi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jwi RCSB], [http://www.ebi.ac.uk/pdbsum/4jwi 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/CTHL3_SHEEP CTHL3_SHEEP]] Exerts, in vitro, a potent antimicrobial activity. Probably due to an impairment of the function of the respiratory chain and of energy-dependent activities in the inner membrane of susceptible microorganisms (By similarity). | [[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/CTHL3_SHEEP CTHL3_SHEEP]] Exerts, in vitro, a potent antimicrobial activity. Probably due to an impairment of the function of the respiratory chain and of energy-dependent activities in the inner membrane of susceptible microorganisms (By similarity). | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial resistance against common antibiotics is an increasing health problem. New pharmaceuticals for the treatment of infections caused by resistant pathogens are needed. Small proline-rich antimicrobial peptides (PrAMPs) from insects are known to bind intracellularly to the conventional substrate binding cleft of the E. coli Hsp70 chaperone DnaK. Furthermore, bactenecins from mammals, members of the cathelicidin family, also contain potential DnaK binding sites. Crystal structures of bovine and sheep Bac7 in complex with the DnaK substrate binding domain show that the peptides bind in the forward binding mode with a leucine positioned in the central hydrophobic pocket. In most structures, proline and arginine residues preceding leucine occupy the hydrophobic DnaK binding sites -1 and -2. Within bovine Bac7, four potential DnaK binding sites were identified. | |||
Structural Identification of DnaK Binding Sites Within Bovine and Sheep Bactenecin Bac7.,Zahn M, Kieslich B, Berthold N, Knappe D, Hoffmann R, Strater N Protein Pept Lett. 2013 Oct 25. PMID:24164259<ref>PMID:24164259</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
[[Category: Straeter, N | [[Category: Straeter, N]] | ||
[[Category: Zahn, M | [[Category: Zahn, M]] | ||
[[Category: Antimicrobial peptide]] | [[Category: Antimicrobial peptide]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Chaperone-antibiotic complex]] | [[Category: Chaperone-antibiotic complex]] | ||
[[Category: Peptide binding]] | [[Category: Peptide binding]] | ||
Revision as of 22:33, 24 December 2014
Crystal structure of the substrate binding domain of E.coli DnaK in complex with sheep Bac7(35-43)Crystal structure of the substrate binding domain of E.coli DnaK in complex with sheep Bac7(35-43)
Structural highlights
Function[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] [CTHL3_SHEEP] Exerts, in vitro, a potent antimicrobial activity. Probably due to an impairment of the function of the respiratory chain and of energy-dependent activities in the inner membrane of susceptible microorganisms (By similarity). Publication Abstract from PubMedBacterial resistance against common antibiotics is an increasing health problem. New pharmaceuticals for the treatment of infections caused by resistant pathogens are needed. Small proline-rich antimicrobial peptides (PrAMPs) from insects are known to bind intracellularly to the conventional substrate binding cleft of the E. coli Hsp70 chaperone DnaK. Furthermore, bactenecins from mammals, members of the cathelicidin family, also contain potential DnaK binding sites. Crystal structures of bovine and sheep Bac7 in complex with the DnaK substrate binding domain show that the peptides bind in the forward binding mode with a leucine positioned in the central hydrophobic pocket. In most structures, proline and arginine residues preceding leucine occupy the hydrophobic DnaK binding sites -1 and -2. Within bovine Bac7, four potential DnaK binding sites were identified. Structural Identification of DnaK Binding Sites Within Bovine and Sheep Bactenecin Bac7.,Zahn M, Kieslich B, Berthold N, Knappe D, Hoffmann R, Strater N Protein Pept Lett. 2013 Oct 25. PMID:24164259[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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