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4ani

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Structural basis for the intermolecular communication between DnaK and GrpE in the DnaK chaperone system from Geobacillus kaustophilus HTA426

Structural highlights

4ani is a 8 chain structure with sequence from Geobacillus kaustophilus HTA426. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 4.094Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GRPE_GEOKA 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 (By similarity).

Publication Abstract from PubMed

The conserved, ATP-dependent bacterial DnaK chaperones process client substrates with the aid of the co-chaperones DnaJ and GrpE. However, in the absence of structural information, how these proteins communicate with each other cannot be fully delineated. For the study reported here, we solved the crystal structure of a full-length Geobacillus kaustophilus HTA426 GrpE homodimer in complex with a nearly full-length G. kaustophilus HTA426 DnaK that contains the interdomain linker (acting as a pseudo-substrate), and the N-terminal nucleotide-binding and C-terminal substrate-binding domains at 4.1-A resolution. Each complex contains two DnaKs and two GrpEs, which is a stoichiometry that has not been found before. The long N-terminal GrpE alpha-helices stabilize the linker of DnaK in the complex. Furthermore, interactions between the DnaK substrate-binding domain and the N-terminal disordered region of GrpE may accelerate substrate release from DnaK. These findings provide molecular mechanisms for substrate binding, processing, and release during the Hsp70 chaperone cycle.

Crystal Structure of DnaK Protein Complexed with Nucleotide Exchange Factor GrpE in DnaK Chaperone System: INSIGHT INTO INTERMOLECULAR COMMUNICATION.,Wu CC, Naveen V, Chien CH, Chang YW, Hsiao CD J Biol Chem. 2012 Jun 15;287(25):21461-70. Epub 2012 Apr 27. PMID:22544739^[1]

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

References

↑ Wu CC, Naveen V, Chien CH, Chang YW, Hsiao CD. Crystal Structure of DnaK Protein Complexed with Nucleotide Exchange Factor GrpE in DnaK Chaperone System: INSIGHT INTO INTERMOLECULAR COMMUNICATION. J Biol Chem. 2012 Jun 15;287(25):21461-70. Epub 2012 Apr 27. PMID:22544739 doi:10.1074/jbc.M112.344358

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ani"

@@ Line 3: / Line 3: @@
 <StructureSection load='4ani' size='340' side='right'caption='[[4ani]], [[Resolution|resolution]] 4.09&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ani]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Geoka Geoka]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ANI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ANI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ani]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_kaustophilus_HTA426 Geobacillus kaustophilus HTA426]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ANI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ANI FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2v7y|2v7y]]</div></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]] 4.094&#8491;</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=4ani FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ani OCA], [https://pdbe.org/4ani PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ani RCSB], [https://www.ebi.ac.uk/pdbsum/4ani PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ani ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GRPE_GEOKA GRPE_GEOKA]] 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 (By similarity). [[https://www.uniprot.org/uniprot/DNAK_GEOKA DNAK_GEOKA]] Acts as a chaperone (By similarity).
+[https://www.uniprot.org/uniprot/GRPE_GEOKA GRPE_GEOKA] 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 (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Geoka]]
+[[Category: Geobacillus kaustophilus HTA426]]
 [[Category: Large Structures]]
-[[Category: Chang, Y W]]
+[[Category: Chang Y-W]]
-[[Category: Chien, C H]]
+[[Category: Chien C-H]]
-[[Category: Hsiao, C D]]
+[[Category: Hsiao C-D]]
-[[Category: Naveen, V]]
+[[Category: Naveen V]]
-[[Category: Wu, C C]]
+[[Category: Wu C-C]]
-[[Category: Chaperone]]
-[[Category: Chaperone cycle]]
-[[Category: Complementary assay]]

4ani

From Proteopedia

Current revision

Structural basis for the intermolecular communication between DnaK and GrpE in the DnaK chaperone system from Geobacillus kaustophilus HTA426

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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