View source for 9blt


==Structure of the human mitochondrial Hsp70 (mortalin; R126W mutant) bound to nucleotide exchange factor GrpEL1 (Y173A mutant)==
<StructureSection load='9blt' size='340' side='right'caption='[[9blt]], [[Resolution|resolution]] 3.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9blt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BLT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.38&#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=9blt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9blt OCA], [https://pdbe.org/9blt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9blt RCSB], [https://www.ebi.ac.uk/pdbsum/9blt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9blt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GRP75_HUMAN GRP75_HUMAN] Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Maintenance of protein homeostasis is necessary for cell viability and depends on a complex network of chaperones and co-chaperones, including the heat-shock protein 70 (Hsp70) system. In human mitochondria, mitochondrial Hsp70 (mortalin) and the nucleotide exchange factor (GrpEL1) work synergistically to stabilize proteins, assemble protein complexes, and facilitate protein import. However, our understanding of the molecular mechanisms guiding these processes is hampered by limited structural information. To elucidate these mechanistic details, we used cryoEM to determine structures of full-length human mortalin-GrpEL1 complexes in previously unobserved states. Our structures and molecular dynamics simulations allow us to delineate specific roles for mortalin-GrpEL1 interfaces and to identify steps in GrpEL1-mediated nucleotide and substrate release by mortalin. Subsequent analyses reveal conserved mechanisms across bacteria and mammals and facilitate a complete understanding of sequential nucleotide and substrate release for the Hsp70 chaperone system.

Structural insights into GrpEL1-mediated nucleotide and substrate release of human mitochondrial Hsp70.,Morizono MA, McGuire KL, Birouty NI, Herzik MA Jr Nat Commun. 2024 Dec 30;15(1):10815. doi: 10.1038/s41467-024-54499-1. PMID:39737924<ref>PMID:39737924</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9blt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Birouty NI]]
[[Category: Herzik Jr MA]]
[[Category: McGuire KL]]
[[Category: Morizono MA]]