Sandbox Eric Martz
From Proteopedia
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:
| N | C |
Color traces by chain:
RING (A) Cullin (C) NEDD8 (A)
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
- ↑ 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.
