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Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

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Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. / Plechanovová, Anna; Jaffray, Ellis G.; Tatham, Michael H.; Naismith, James H.; Hay, Ronald T. (Lead / Corresponding author).

In: Nature, Vol. 489, No. 7414, 2012, p. 115-120.

Research output: Contribution to journalArticle

Harvard

Plechanovová, A, Jaffray, EG, Tatham, MH, Naismith, JH & Hay, RT 2012, 'Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis' Nature, vol 489, no. 7414, pp. 115-120.

APA

Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., & Hay, R. T. (2012). Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature, 489(7414), 115-120doi: 10.1038/nature11376

Vancouver

Plechanovová A, Jaffray EG, Tatham MH, Naismith JH, Hay RT. Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature. 2012;489(7414):115-120.

Author

Plechanovová, Anna; Jaffray, Ellis G.; Tatham, Michael H.; Naismith, James H.; Hay, Ronald T. (Lead / Corresponding author) / Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis.

In: Nature, Vol. 489, No. 7414, 2012, p. 115-120.

Research output: Contribution to journalArticle

Bibtex - Download

@article{23989cc0bd7e410bb8520c2d2537d713,
title = "Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis",
author = "Anna Plechanovová and Jaffray, {Ellis G.} and Tatham, {Michael H.} and Naismith, {James H.} and Hay, {Ronald T.}",
year = "2012",
volume = "489",
number = "7414",
pages = "115--120",
journal = "Nature",
issn = "0028-0836",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

A1 - Plechanovová,Anna

A1 - Jaffray,Ellis G.

A1 - Tatham,Michael H.

A1 - Naismith,James H.

A1 - Hay,Ronald T.

AU - Plechanovová,Anna

AU - Jaffray,Ellis G.

AU - Tatham,Michael H.

AU - Naismith,James H.

AU - Hay,Ronald T.

PY - 2012

Y1 - 2012

N2 - Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 conjugating enzyme linked to ubiquitin via a thioester bond, but the mechanism of transfer has remained elusive. Here we report the crystal structure of the dimeric RING domain of rat RNF4 in complex with E2 (UbcH5A) linked by an isopeptide bond to ubiquitin. While the E2 contacts a single protomer of the RING, ubiquitin is folded back onto the E2 by contacts from both RING protomers. The carboxy-terminal tail of ubiquitin is locked into an active site groove on the E2 by an intricate network of interactions, resulting in changes at the E2 active site. This arrangement is primed for catalysis as it can deprotonate the incoming substrate lysine residue and stabilize the consequent tetrahedral transition-state intermediate.

AB - Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 conjugating enzyme linked to ubiquitin via a thioester bond, but the mechanism of transfer has remained elusive. Here we report the crystal structure of the dimeric RING domain of rat RNF4 in complex with E2 (UbcH5A) linked by an isopeptide bond to ubiquitin. While the E2 contacts a single protomer of the RING, ubiquitin is folded back onto the E2 by contacts from both RING protomers. The carboxy-terminal tail of ubiquitin is locked into an active site groove on the E2 by an intricate network of interactions, resulting in changes at the E2 active site. This arrangement is primed for catalysis as it can deprotonate the incoming substrate lysine residue and stabilize the consequent tetrahedral transition-state intermediate.

U2 - 10.1038/nature11376

DO - 10.1038/nature11376

M1 - Article

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7414

VL - 489

SP - 115

EP - 120

ER -

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