PDBsum entry 4q5e

Unknown function, protein binding

PDB id: 4q5e

Contents

Protein chains

168 a.a.

76 a.a.

155 a.a.

Waters ×237

PDB id:

4q5e

Name:

Unknown function, protein binding

Title:

Shigella effector kinase ospg bound to e2-ub ubch7-ub conjugate

Structure:

Protein kinase ospg. Chain: a. Fragment: unp residues 26-193. Synonym: effector protein ospg. Engineered: yes. Polyubiquitin. Chain: b. Synonym: ubiquitin. Engineered: yes.

Source:

Shigella sonnei ss046. Organism_taxid: 300269. Strain: 2457t. Gene: ospg, sson_p170. Expressed in: escherichia coli. Expression_system_taxid: 469008. Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292.

Resolution:

1.87Å R-factor: 0.187 R-free: 0.232

Authors:

M.Cygler,A.M.Grishin,Montreal-Kingston Bacterial Structural Genomics Initiative (Bsgi)

Key ref:

A.M.Grishin et al. (2014). Structural basis for the inhibition of host protein ubiquitination by Shigella effector kinase OspG. Structure, 22, 878-888. PubMed id: 24856362 DOI: 10.1016/j.str.2014.04.010

Date:

16-Apr-14 Release date: 02-Jul-14

Protein chain

Q3YTH2  (OSPG_SHISS) -  Protein kinase OspG from Shigella sonnei (strain Ss046)

Seq: 196 a.a.

Struc: 168 a.a.

Protein chain

P0CG63  (UBI4P_YEAST) -  Polyubiquitin from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 381 a.a.

Struc: 76 a.a.*

Protein chain

P68036  (UB2L3_HUMAN) -  Ubiquitin-conjugating enzyme E2 L3 from Homo sapiens

Seq: 154 a.a.

Struc: 155 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chain A: E.C.2.7.-.-
• Enzyme class 3: Chain B: E.C.6.3.2.19 - Transferred entry: 2.3.2.23, 2.3.2.27 and 6.2.1.45.
• Reaction: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine
• Enzyme class 4: Chain C: E.C.2.3.2.23 - E2 ubiquitin-conjugating enzyme.
• Reaction: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine

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.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2014.04.010

Structure 22:878-888 (2014)

PubMed id: 24856362

Structural basis for the inhibition of host protein ubiquitination by Shigella effector kinase OspG.

A.M.Grishin, T.E.Condos, K.R.Barber, F.X.Campbell-Valois, C.Parsot, G.S.Shaw, M.Cygler.

ABSTRACT

Shigella invasion of its human host is assisted by T3SS-delivered effector proteins. The OspG effector kinase binds ubiquitin and ubiquitin-loaded E2-conjugating enzymes, including UbcH5b and UbcH7, and attenuates the host innate immune NF-kB signaling. We present the structure of OspG bound to the UbcH7∼Ub conjugate. OspG has a minimal kinase fold lacking the activation loop of regulatory kinases. UbcH7∼Ub binds OspG at sites remote from the kinase active site, yet increases its kinase activity. The ubiquitin is positioned in the "open" conformation with respect to UbcH7 using its I44 patch to interact with the C terminus of OspG. UbcH7 binds to OspG using two conserved loops essential for E3 ligase recruitment. The interaction of the UbcH7∼Ub with OspG is remarkably similar to the interaction of an E2∼Ub with a HECT E3 ligase. OspG interferes with the interaction of UbcH7 with the E3 parkin and inhibits the activity of the E3.