PDBsum entry 4fk5

Hydrolase

PDB id: 4fk5

Contents

Protein chains

437 a.a.

92 a.a.

92 a.a.

91 a.a.

Ligands

GOL ×2

EDO

Metals

_ZN ×8

Waters ×396

PDB id:

4fk5

Name:

Hydrolase

Title:

Structure of the saga ubp8(s144n)/sgf11/sus1/sgf73 dub module

Structure:

Ubiquitin carboxyl-terminal hydrolase 8. Chain: a. Synonym: deubiquitinating enzyme 8, ubiquitin thioesterase 8, ubiquitin-specific-processing protease 8. Engineered: yes. Mutation: yes. Protein sus1. Chain: b. Engineered: yes.

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: ubp8, ym9959.05, ymr223w. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: sus1, ybr111w-a. Gene: sgf11, ypl047w.

Resolution:

2.03Å R-factor: 0.177 R-free: 0.212

Authors:

N.L.Samara,A.E.Ringel,C.Wolberger

Key ref:

N.L.Samara et al. (2012). A role for intersubunit interactions in maintaining SAGA deubiquitinating module structure and activity. Structure, 20, 1414-1424. PubMed id: 22771212

Date:

12-Jun-12 Release date: 25-Jul-12

Protein chain

P50102  (UBP8_YEAST) -  Ubiquitin carboxyl-terminal hydrolase 8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 471 a.a.

Struc: 437 a.a.*

Protein chain

Q6WNK7  (SUS1_YEAST) -  Transcription and mRNA export factor SUS1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 96 a.a.

Struc: 92 a.a.

Protein chain

Q03067  (SGF11_YEAST) -  SAGA-associated factor 11 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 99 a.a.

Struc: 92 a.a.

Protein chain

P53165  (SGF73_YEAST) -  SAGA-associated factor 73 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 657 a.a.

Struc: 91 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 2: Chain A: E.C.3.4.19.12 - ubiquitinyl hydrolase 1.
• Reaction: Thiol-dependent hydrolysis of ester, thiolester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
• Enzyme class 3: Chains B, C, E: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Structure 20:1414-1424 (2012)

PubMed id: 22771212

A role for intersubunit interactions in maintaining SAGA deubiquitinating module structure and activity.

N.L.Samara, A.E.Ringel, C.Wolberger.

ABSTRACT

No abstract given.