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PDBsum entry 3u5o

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protein metals Protein-protein interface(s) links
Transcription PDB id
3u5o

 

 

 

 

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Contents
Protein chains
(+ 2 more) 189 a.a.
(+ 2 more) 20 a.a.
Metals
_ZN ×16
PDB id:
3u5o
Name: Transcription
Title: Crystal structure of the complex of trim33 phd-bromo and h3(1-22) k9me3k14ack18ac histone peptide
Structure: E3 ubiquitin-protein ligase trim33. Chain: a, b, c, d, e, f, g, h. Fragment: the phd and bromo domain of trim33. Synonym: ectodermin homolog, ret-fused gene 7 protein, protein rfg7, transcription intermediary factor 1-gamma, tif1-gamma, tripartite motif-containing protein 33. Engineered: yes. Histone h3.1. Chain: i, j, k, l, m, n, o, p.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: trim33, kiaa1113, rfg7, tif1g. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: this sequence occurs naturally in humans
Resolution:
2.70Å     R-factor:   0.207     R-free:   0.280
Authors: Z.Wang,D.J.Patel
Key ref: Q.Xi et al. (2011). A poised chromatin platform for TGF-β access to master regulators. Cell, 147, 1511-1524. PubMed id: 22196728
Date:
11-Oct-11     Release date:   18-Jan-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9UPN9  (TRI33_HUMAN) -  E3 ubiquitin-protein ligase TRIM33 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1127 a.a.
189 a.a.
Protein chains
Pfam   ArchSchema ?
P68431  (H31_HUMAN) -  Histone H3.1 from Homo sapiens
Seq:
Struc:
136 a.a.
20 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chains A, B, C, D, E, F, G, H: 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: Chains I, J, K, L, M, N, O, P: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
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.

 

 
Cell 147:1511-1524 (2011)
PubMed id: 22196728  
 
 
A poised chromatin platform for TGF-β access to master regulators.
Q.Xi, Z.Wang, A.I.Zaromytidou, X.H.Zhang, L.F.Chow-Tsang, J.X.Liu, H.Kim, A.Barlas, K.Manova-Todorova, V.Kaartinen, L.Studer, W.Mark, D.J.Patel, J.Massagué.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23211769 C.A.Musselman, M.E.Lalonde, J.Côté, and T.G.Kutateladze (2012).
Perceiving the epigenetic landscape through histone readers.
  Nat Struct Mol Biol, 19, 1218-1227.  
22992590 J.Massagué (2012).
TGFβ signalling in context.
  Nat Rev Mol Cell Biol, 13, 616-630.  
22743709 K.Aggarwal, and J.Massagué (2012).
Ubiquitin removal in the TGF-β pathway.
  Nat Cell Biol, 14, 656-657.  
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.

 

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