Search Results

You searched for all publications:

with publication states 'Published (Approved)'

Search Again...

These results only include publications that have been reviewed and processed by Diamond Light Source. To also view papers that have not yet been processed click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

Exact matches
Related results

3 items found (0 items not approved), displaying all items.1

Instruments / Technical Area	Publication Details	Published
Krios II-Titan Krios II at Diamond	Insights into centromere DNA bending revealed by the cryo-EM structure of the core centromere binding factor 3 with Ndc10 Wenjuan Zhang , Natalya Lukoyanova , Shomon Miah , Jonathan Lucas , Cara K. Vaughan Cell Reports 24, 744 - 754 DOI: 10.1016/j.celrep.2018.06.068 Diamond Proposal Number(s): [14704, 15619] Open Access Show Abstract ▼ Abstract: The centromere binding factor 3 (CBF3) complex binds the third centromere DNA element in organisms with point centromeres, such as S. cerevisiae. It is an essential complex for assembly of the kinetochore in these organisms, as it facilitates genetic centromere specification and allows association of all other kinetochore components. We determined high-resolution structures of the core complex of CBF3 alone and in association with a monomeric construct of Ndc10, using cryoelectron microscopy (cryo-EM). We identify the DNA-binding site of the complex and present a model in which CBF3 induces a tight bend in centromeric DNA, thus facilitating assembly of the centromeric nucleosome.	Jul 2018
I04-Macromolecular Crystallography	The crystal structure of the Sgt1-Skp1 complex: the link between Hsp90 and both SCF E3 ubiquitin ligases and kinetochores Oliver Willhoft , Richard Kerr , Dipali Patel , Wenjuan Zhang , Caezar Al-Jassar , Tina Daviter , Stefan H. Millson , Konstantinos Thalassinos , Cara K. Vaughan Scientific Reports 7 DOI: 10.1038/srep41626 Open Access Show Abstract ▼ Abstract: The essential cochaperone Sgt1 recruits Hsp90 chaperone activity to a range of cellular factors including SCF E3 ubiquitin ligases and the kinetochore in eukaryotes. In these pathways Sgt1 interacts with Skp1, a small protein that heterodimerizes with proteins containing the F-box motif. We have determined the crystal structure of the interacting domains of Saccharomyces cerevisiae Sgt1 and Skp1 at 2.8 Å resolution and validated the interface in the context of the full-length proteins in solution. The BTB/POZ domain of Skp1 associates with Sgt1 via the concave surface of its TPR domain using residues that are conserved in humans. Dimerization of yeast Sgt1 occurs via an insertion that is absent from monomeric human Sgt1. We identify point mutations that disrupt dimerization and Skp1 binding in vitro and find that the interaction with Skp1 is an essential function of Sgt1 in yeast. Our data provide a structural rationale for understanding the phenotypes of temperature-sensitive Sgt1 mutants and for linking Skp1-associated proteins to Hsp90-dependent pathways.	Jan 2017
I24-Microfocus Macromolecular Crystallography	Structural and functional basis of protein phosphatase 5 substrate specificity Jasmeen Oberoi , Diana M. Dunn , Mark R. Woodford , Laura Mariotti , Jacqualyn Schulman , Dimitra Bourboulia , Mehdi Mollapour , Cara K. Vaughan Proceedings Of The National Academy Of Sciences 113, 9009 - 9014 DOI: 10.1073/pnas.1603059113 Diamond Proposal Number(s): [7197] Show Abstract ▼ Abstract: The serine/threonine phosphatase protein phosphatase 5 (PP5) regulates hormone- and stress-induced cellular signaling by association with the molecular chaperone heat shock protein 90 (Hsp90). PP5-mediated dephosphorylation of the cochaperone Cdc37 is essential for activation of Hsp90-dependent kinases. However, the details of this mechanism remain unknown. We determined the crystal structure of a Cdc37 phosphomimetic peptide bound to the catalytic domain of PP5. The structure reveals PP5 utilization of conserved elements of phosphoprotein phosphatase (PPP) structure to bind substrate and provides a template for many PPP–substrate interactions. Our data show that, despite a highly conserved structure, elements of substrate specificity are determined within the phosphatase catalytic domain itself. Structure-based mutations in vivo reveal that PP5-mediated dephosphorylation is required for kinase and steroid hormone receptor release from the chaperone complex. Finally, our data show that hyper- or hypoactivity of PP5 mutants increases Hsp90 binding to its inhibitor, suggesting a mechanism to enhance the efficacy of Hsp90 inhibitors by regulation of PP5 activity in tumors.	Aug 2016

Publications Database

Search Results

You searched for all publications:

Search Again...

Subject Areas (check all that apply) select all

Instruments used to collect data (check all that apply) select all

Collaborations involved (check all that apply) select all

Diamond Offline Facilities used

Relevant Technical Areas (check all that apply) select all

Menu for Anonymous User