5obv

Mycoplasma genitalium DnaK deletion mutant lacking SBDalpha in complex with ADP and Pi.

spinqualitylabelsall models 5obv, resolution 2.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5obv is a 1 chain structure with sequence from Mycoplasma genitalium G37. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.49Å Ligands: ADP, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DNAK_MYCGE Acts as a chaperone. Publication Abstract from PubMed Hsp70 chaperones keep protein homeostasis facilitating the response of organisms to changes in external and internal conditions. Hsp70s have two domains-nucleotide binding domain (NBD) and substrate binding domain (SBD)-connected by a conserved hydrophobic linker. Functioning of Hsp70s depend on tightly regulated cycles of ATP hydrolysis allosterically coupled, often together with cochaperones, to the binding/release of peptide substrates. Here we describe the crystal structure of the Mycoplasma genitalium DnaK (MgDnaK) protein, an Hsp70 homolog, in the noncompact, nucleotide-bound/substrate-bound conformation. The MgDnaK structure resembles the one from the thermophilic eubacteria DnaK trapped in the same state. However, in MgDnaK the NBD and SBD domains remain close to each other despite the lack of direct interaction between them and with the linker contacting the two subdomains of SBD. These observations suggest that the structures might represent an intermediate of the protein where the conserved linker binds to the SBD to favor the noncompact state of the protein by stabilizing the SBDbeta-SBDalpha subdomains interaction, promoting the capacity of the protein to sample different conformations, which is critical for proper functioning of the molecular chaperone allosteric mechanism. Comparison of the solved structures indicates that the NBD remains essentially invariant in presence or absence of nucleotide. The nucleotide-bound/substrate-bound conformation of the Mycoplasma genitalium DnaK chaperone.,Adell M, Calisto BM, Fita I, Martinelli L Protein Sci. 2018 May;27(5):1000-1007. doi: 10.1002/pro.3401. Epub 2018 Apr 14. PMID:29520883 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Protein structures

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