Reference: Nakamura Y, et al. (2007) Purification, crystallization and preliminary X-ray diffraction analysis of the non-ATPase subunit Nas6 in complex with the ATPase subunit Rpt3 of the 26S proteasome from Saccharomyces cerevisiae. Acta Crystallogr Sect F Struct Biol Cryst Commun 63(Pt 3):190-2

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Abstract


The non-ATPase subunit Nas6, which is the human orthologue of gankyrin, was co-expressed with the C-terminal domain of the ATPase subunit Rpt3 of the yeast 26S proteasome in Escherichia coli, purified to near-homogeneity and crystallized using the hanging-drop vapour-diffusion method. The protein crystallized in space group P2(1), with unit-cell parameters a = 60.38, b = 100.22, c = 72.20 A, beta = 94.70 degrees and with three Nas6-Rpt3C molecules per asymmetric unit. The crystal diffracted to beyond 2.2 A resolution using synchrotron radiation.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Nakamura Y, Umehara T, Tanaka A, Horikoshi M, Padmanabhan B, Yokoyama S
Primary Lit For
RPT3 | NAS6

Interaction Annotations


Genetic Interactions

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Interactor Interactor Allele Assay Annotation Action Phenotype SGA score P-value Source Reference

Physical Interactions 1 entry for 2 genes

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InteractorInteractorAssayAnnotationActionModification
RPT3NAS6Co-crystal Structuremanually curatedHit-BaitNo Modification
Showing 1 to 1 of 1 entries