1dkg

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Revision as of 09:28, 21 July 2021

CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO THE ATPASE DOMAIN OF THE MOLECULAR CHAPERONE DNAK

Structural highlights

1dkg is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. The August 2002 RCSB PDB Molecule of the Month feature on Chaperones by David S. Goodsell is 10.2210/rcsb_pdb/mom_2002_8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GRPE_ECOLI] Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.^[1] ^[2] ^[3] ^[4] [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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK [heat shock protein 70 (Hsp70)] was determined at 2.8 angstrom resolution. A dimer of GrpE binds asymmetrically to a single molecule of DnaK. The structure of the nucleotide-free ATPase domain in complex with GrpE resembles closely that of the nucleotide-bound mammalian Hsp70 homolog, except for an outward rotation of one of the subdomains of the protein. This conformational change is not consistent with tight nucleotide binding. Two long alpha helices extend away from the GrpE dimer and suggest a role for GrpE in peptide release from DnaK.

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.,Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J Science. 1997 Apr 18;276(5311):431-5. PMID:9103205^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2874-8. PMID:1826368
↑ Wu B, Wawrzynow A, Zylicz M, Georgopoulos C. Structure-function analysis of the Escherichia coli GrpE heat shock protein. EMBO J. 1996 Sep 16;15(18):4806-16. PMID:8890154
↑ Mehl AF, Heskett LD, Neal KM. A GrpE mutant containing the NH(2)-terminal "tail" region is able to displace bound polypeptide substrate from DnaK. Biochem Biophys Res Commun. 2001 Mar 30;282(2):562-9. PMID:11401497 doi:http://dx.doi.org/10.1006/bbrc.2001.4567
↑ Brehmer D, Gassler C, Rist W, Mayer MP, Bukau B. Influence of GrpE on DnaK-substrate interactions. J Biol Chem. 2004 Jul 2;279(27):27957-64. Epub 2004 Apr 21. PMID:15102842 doi:http://dx.doi.org/10.1074/jbc.M403558200
↑ Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science. 1997 Apr 18;276(5311):431-5. PMID:9103205

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dkg"

@@ Line 3: / Line 3: @@
 <StructureSection load='1dkg' size='340' side='right'caption='[[1dkg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dkg]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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=1DKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DKG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dkg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The August 2002 RCSB PDB [https://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 [https://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=1DKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DKG 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=1dkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkg OCA], [http://pdbe.org/1dkg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dkg RCSB], [http://www.ebi.ac.uk/pdbsum/1dkg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dkg ProSAT]</span></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=1dkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkg OCA], [https://pdbe.org/1dkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dkg RCSB], [https://www.ebi.ac.uk/pdbsum/1dkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dkg ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GRPE_ECOLI GRPE_ECOLI]] Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.<ref>PMID:1826368</ref> <ref>PMID:8890154</ref> <ref>PMID:11401497</ref> <ref>PMID:15102842</ref>  [[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]
+[[https://www.uniprot.org/uniprot/GRPE_ECOLI GRPE_ECOLI]] Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.<ref>PMID:1826368</ref> <ref>PMID:8890154</ref> <ref>PMID:11401497</ref> <ref>PMID:15102842</ref>  [[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]]

1dkg

From Proteopedia

Revision as of 09:28, 21 July 2021

CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO THE ATPASE DOMAIN OF THE MOLECULAR CHAPERONE DNAK

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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