1dkz

<StructureSection load='1dkz' size='340' side='right' caption='[[1dkz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1dkz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The August 2002 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Chaperones'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2002_8 10.2210/rcsb_pdb/mom_2002_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DKZ FirstGlance]. <br>

</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=1dkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkz OCA], [http://pdbe.org/1dkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dkz RCSB], [http://www.ebi.ac.uk/pdbsum/1dkz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dkz ProSAT]</span></td></tr>

[[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]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dk/1dkz_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 angstroms resolution. The structure consists of a beta-sandwich subdomain followed by alpha-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the beta sandwich. An alpha-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes.

Structural analysis of substrate binding by the molecular chaperone DnaK.,Zhu X, Zhao X, Burkholder WF, Gragerov A, Ogata CM, Gottesman ME, Hendrickson WA Science. 1996 Jun 14;272(5268):1606-14. PMID:8658133<ref>PMID:8658133</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1dkz" style="background-color:#fffaf0;"></div>

*[[Heat Shock Proteins|Heat Shock Proteins]]

[[Category: Burkholder, W F]]

[[Category: Gottesman, M E]]

[[Category: Gragerov, A]]

[[Category: Hendrickson, W A]]

[[Category: Ogata, C M]]

[[Category: Zhao, X]]

[[Category: Zhu, X]]

[[Category: Dnak]]