PDBsum entry 4r7e

Ligase

PDB id

4r7e

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Contents

			Protein chain

					69 a.a.

			Metals

					_ZN ×2

			Waters ×9

PDB id:

4r7e

Links

Name:

Ligase

Title:

Structure of bre1 ring domain

Structure:

E3 ubiquitin-protein ligase bre1. Chain: a. Fragment: ring domain (unp residues 632-700). Synonym: brefeldin a-sensitivity protein 1. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: bre1, ydl074c. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.25Å

R-factor:

0.223

R-free:

0.247

Authors:

P.Kumar,C.Wolberger

Key ref:

P.Kumar and C.Wolberger (2015). Structure of the yeast Bre1 RING domain. Proteins, 83, 1185-1190. PubMed id: 25864391 DOI: 10.1002/prot.24812

Date:

27-Aug-14

Release date:

13-May-15

PROCHECK

	Headers

	References

Protein chain

Q07457 (BRE1_YEAST) - E3 ubiquitin-protein ligase BRE1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: Struc:

Seq: Struc:					700 a.a. 69 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.3.2.27 - RING-type E3 ubiquitin transferase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆- ubiquitinyl-[acceptor protein]-L-lysine

DOI no: 10.1002/prot.24812	Proteins 83:1185-1190 (2015)
PubMed id: 25864391

Structure of the yeast Bre1 RING domain.
P.Kumar, C.Wolberger.

ABSTRACT

Monoubiquitination of histone H2B at Lys123 in yeast plays a critical role in regulating transcription, mRNA export, DNA replication, and the DNA damage response. The RING E3 ligase, Bre1, catalyzes monoubiquitination of H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The crystal structure of a C-terminal fragment of Bre1 shows that the catalytic RING domain is preceded by an N-terminal helix that mediates coiled-coil interactions with a crystallographically related monomer. Homology modeling suggests that the human homologue of Bre1, RNF20/RNF40, heterodimerizes through similar coiled-coil interactions. Proteins 2015; 83:1185-1190. © 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.