 |
PDBsum entry 4npn
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein transport
|
PDB id
|
|
|
|
4npn
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Protein transport
|
|
|
Title:
|
|
Crystal structure of human tetra-sumo-2
|
|
Structure:
|
|
Small ubiquitin-related modifier 2. Chain: a. Fragment: deltan11sumo-2, unp residues 12-93. Synonym: sumo-2, hsmt3, smt3 homolog 2, sumo-3, sentrin-2, ubiquitin- like protein smt3a, smt3a. Engineered: yes
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Gene: smt3a, smt3h2, sumo2, sumo2 smt3a smt3h2. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
Resolution:
|
|
|
1.63Å
|
R-factor:
|
0.199
|
R-free:
|
0.218
|
|
|
Authors:
|
|
C.C.-H.Kung,M.T.Naik,C.L.Chen,C.Ma,T.H.Huang
|
|
Key ref:
|
|
C.C.Kung
et al.
(2014).
Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domain.
Biochem J,
462,
53-65.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
22-Nov-13
|
Release date:
|
15-Oct-14
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P61956
(SUMO2_HUMAN) -
Small ubiquitin-related modifier 2 from Homo sapiens
|
|
|
|
Seq:
Struc:
|
|
|
|
95 a.a.
71 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Biochem J
462:53-65
(2014)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domain.
|
|
C.C.Kung,
M.T.Naik,
S.H.Wang,
H.M.Shih,
C.C.Chang,
L.Y.Lin,
C.L.Chen,
C.Ma,
C.F.Chang,
T.H.Huang.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The E3 ubiquitin ligase RNF4 (RING finger protein 4) contains four tandem SIM
[SUMO (small ubiquitin-like modifier)-interaction motif] repeats for selective
interaction with poly-SUMO-modified proteins, which it targets for degradation.
We employed a multi-faceted approach to characterize the structure of the
RNF4-SIMs domain and the tetra-SUMO2 chain to elucidate the interaction between
them. In solution, the SIM domain was intrinsically disordered and the linkers
of the tetra-SUMO2 were highly flexible. Individual SIMs of the RNF4-SIMs
domains bind to SUMO2 in the groove between the β2-strand and the α1-helix
parallel to the β2-strand. SIM2 and SIM3 bound to SUMO with a high affinity and
together constituted the recognition module necessary for SUMO binding. SIM4
alone bound to SUMO with low affinity; however, its contribution to tetra-SUMO2
binding avidity is comparable with that of SIM3 when in the RNF4-SIMs domain.
The SAXS data of the tetra-SUMO2-RNF4-SIMs domain complex indicate that it
exists as an ordered structure. The HADDOCK model showed that the tandem
RNF4-SIMs domain bound antiparallel to the tetra-SUMO2 chain orientation and
wrapped around the SUMO protamers in a superhelical turn without imposing steric
hindrance on either molecule.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
