Sandbox Eric Martz

From Proteopedia

Revision as of 18:59, 22 February 2009

This article is under collaborative development by Eric Martz (UMass) and Raymond J. Deshaies and his team (CalTech). Please do not edit this page unless you are a member of the development team. Once completed, this page may be moved to a permanent article title.

Proposed article title: Release of RING from Cullin by NEDD8ylation

RING (A)   Cullin (C)   NEDD8 (A)

Display chains as smoothed backbone traces colored by N->C Rainbow:

Color traces by chain:

Contacts to:

The morph ^[1] button above shows the transition from a Cullin-RING ligase dimer (3dpl) to the trimer resulting from NEDD8ylation (covalent addition of the NEDD8 ubiquitin-like chain to Lys724 of Cullin; 3dqv). NEDD8 binds and rotates the C-terminal domain of Cullin, releasing the folded RING domain from its Cullin-binding site. RING remains attached to Cullin by the RING N-terminus which remains embedded in Cullin. The contraction and re-expansion of the C-terminal domain during rotation is an artifact of the morphing algorithm.

Notes and References

1. ↑ The 9-model morph file can be downloaded from Image:3dpl 3dqv acr morph.pdb. The morph represents the change from 3dpl to 3dqv, and only chains C and R which are common to these two models. Only one trimer was used from 3dqv (which contains 2 trimers in the asymmetric unit), namely, the one with chains named A, C, and R. This trimer was obtained from PQS as 3dqv_1.mmol. The morph was performed by the Yale Morph Server (beta server), ID b899128-21508. This produced 8 models numbered 0-7. In the product morph, the orientation of the final chains was not changed. Hence, chain A (NEDD8) from 3dqv.pdb was added as model number 8 (9th model) without the need for special alignment. Morph done by Eric Martz at the request of Raymond J. Deshaies of CalTech.