|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of lobe II from the nucleotide binding domain of DnaK in complex with AMPPCP== | | ==Crystal structure of lobe II from the nucleotide binding domain of DnaK in complex with AMPPCP== |
| - | <StructureSection load='5oow' size='340' side='right' caption='[[5oow]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='5oow' size='340' side='right'caption='[[5oow]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oow]] 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=5OOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OOW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oow]] is a 2 chain structure with sequence from [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=5OOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OOW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></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]] 2.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaK, groP, grpF, seg, b0014, JW0013 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></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=5oow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oow OCA], [http://pdbe.org/5oow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oow RCSB], [http://www.ebi.ac.uk/pdbsum/5oow PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oow ProSAT]</span></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=5oow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oow OCA], [https://pdbe.org/5oow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oow RCSB], [https://www.ebi.ac.uk/pdbsum/5oow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oow 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] | + | [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 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5oow" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5oow" 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: Escherichia coli K-12]] |
| - | [[Category: Bauer, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Jakob, R P]] | + | [[Category: Bauer D]] |
| - | [[Category: Maier, T]] | + | [[Category: Jakob RP]] |
| - | [[Category: Meinhold, S]] | + | [[Category: Maier T]] |
| - | [[Category: Merkel, U]] | + | [[Category: Meinhold S]] |
| - | [[Category: Rief, M]] | + | [[Category: Merkel U]] |
| - | [[Category: Stigler, J]] | + | [[Category: Rief M]] |
| - | [[Category: Zoldak, G]] | + | [[Category: Stigler J]] |
| - | [[Category: Chaperone]]
| + | [[Category: Zoldak G]] |
| - | [[Category: Hsp70]]
| + | |
| - | [[Category: Nbd]]
| + | |
| - | [[Category: Nucleotide binding domain]]
| + | |
| - | [[Category: Sugar kinase family]]
| + | |
| 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]
Publication Abstract from PubMed
The folding pathways of large proteins are complex, with many of them requiring the aid of chaperones and others folding spontaneously. Along the folding pathways, partially folded intermediates are frequently populated; their role in the driving of the folding process is unclear. The structures of these intermediates are generally not amenable to high-resolution structural techniques because of their transient nature. Here we employed single-molecule force measurements to scrutinize the hierarchy of intermediate structures along the folding pathway of the nucleotide binding domain (NBD) of Escherichia coli Hsp70 DnaK. DnaK-NBD is a member of the sugar kinase superfamily that includes Hsp70s and the cytoskeletal protein actin. Using optical tweezers, a stable nucleotide-binding competent en route folding intermediate comprising lobe II residues (183-383) was identified as a critical checkpoint for productive folding. We obtained a structural snapshot of this folding intermediate that shows native-like conformation. To assess the fundamental role of folded lobe II for efficient folding, we turned our attention to yeast mitochondrial NBD, which does not fold without a dedicated chaperone. After replacing the yeast lobe II residues with stable E. coli lobe II, the obtained chimeric protein showed native-like ATPase activity and robust folding into the native state, even in the absence of chaperone. In summary, lobe II is a stable nucleotide-binding competent folding nucleus that is the key to time-efficient folding and possibly resembles a common ancestor domain. Our findings provide a conceptual framework for the folding pathways of other members of this protein superfamily.
A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy.,Bauer D, Meinhold S, Jakob RP, Stigler J, Merkel U, Maier T, Rief M, Zoldak G Proc Natl Acad Sci U S A. 2018 Apr 18. pii: 1716899115. doi:, 10.1073/pnas.1716899115. PMID:29669923[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bauer D, Meinhold S, Jakob RP, Stigler J, Merkel U, Maier T, Rief M, Zoldak G. A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy. Proc Natl Acad Sci U S A. 2018 Apr 18. pii: 1716899115. doi:, 10.1073/pnas.1716899115. PMID:29669923 doi:http://dx.doi.org/10.1073/pnas.1716899115
|
