PDBsum entry 4a4b

Ligase/transferase

PDB id

4a4b

Loading ...

Contents

			Protein chains

					388 a.a.


					146 a.a.

			Ligands

					SER-ASP-GLY-PTR- THR-PRO-GLU-PRO- ALA

			Metals

					_CA


					_ZN ×2

			Waters ×17

PDB id:

4a4b

Links

Name:

Ligase/transferase

Title:

Structure of modified phosphotyr371-c-cbl-ubch5b-zap-70 complex

Structure:

E3 ubiquitin-protein ligase cbl. Chain: a. Fragment: tkb domain, linker helix region, and ring domain, residues 47-435. Synonym: casitas b-lineage lymphoma proto-oncogene, proto-oncogenE C- cbl, ring finger protein 55, signal transduction protein cbl, c-cbl. Engineered: yes. Mutation: yes. Tyrosine-protein kinase zap-70.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: gold. Synthetic: yes.

Resolution:

2.79Å

R-factor:

0.191

R-free:

0.267

Authors:

H.Dou,L.Buetow,A.Hock,G.J.Sibbet,K.H.Vousden,D.T.Huang

Key ref:

H.Dou et al. (2012). Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl. Nat Struct Biol, 19, 184-192. PubMed id: 22266821

Date:

08-Oct-11

Release date:

25-Jan-12

PROCHECK

	Headers

	References

Protein chain

P22681 (CBL_HUMAN) - E3 ubiquitin-protein ligase CBL from Homo sapiens

Seq: Struc:

Seq: Struc:					906 a.a. 388 a.a.*

Protein chain

P62837 (UB2D2_HUMAN) - Ubiquitin-conjugating enzyme E2 D2 from Homo sapiens

Seq: Struc:					147 a.a. 146 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

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



		Enzyme reactions

Enzyme class 2:

Chain A: 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

Enzyme class 3:

Chain C: E.C.2.3.2.23 - E2 ubiquitin-conjugating enzyme.

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

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

Enzyme class 4:

Chain C: E.C.2.3.2.24 - (E3-independent) E2 ubiquitin-conjugating enzyme.

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

Reaction:

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N₆- monoubiquitinyl-[acceptor protein]-L-lysine

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.

	Nat Struct Biol 19:184-192 (2012)
PubMed id: 22266821

Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl.
H.Dou, L.Buetow, A.Hock, G.J.Sibbet, K.H.Vousden, D.T.Huang.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

22902369

H.Dou, L.Buetow, G.J.Sibbet, K.Cameron, and D.T.Huang (2012).
BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer.

Nat Struct Mol Biol, 19, 876-883.

PDB code:

4auq

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.