View source for 5obv


==Mycoplasma genitalium DnaK deletion mutant lacking SBDalpha in complex with ADP and Pi.==
<StructureSection load='5obv' size='340' side='right'caption='[[5obv]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5obv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma_genitalium_G37 Mycoplasma genitalium G37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OBV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=5obv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5obv OCA], [https://pdbe.org/5obv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5obv RCSB], [https://www.ebi.ac.uk/pdbsum/5obv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5obv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DNAK_MYCGE DNAK_MYCGE] Acts as a chaperone.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:29520883</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5obv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycoplasma genitalium G37]]
[[Category: Adell M]]
[[Category: Calisto B]]
[[Category: Fita I]]
[[Category: Martinelli L]]