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PDBsum entry 3ldz
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protein Protein-protein interface(s) links
Protein transport PDB id
3ldz

 

 

 

 

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Contents
Protein chains
73 a.a. *
140 a.a. *
* Residue conservation analysis
PDB id:
3ldz
Name: Protein transport
Title: Crystal structure of human stam1 vhs domain in complex with ubiquitin
Structure: Ubiquitin. Chain: f, e, g. Signal transducing adapter molecule 1. Chain: a, d, b, c. Fragment: human stam1 vhs domain. Synonym: stam-1
Source: Bos taurus. Bovine. Organism_taxid: 9913. Homo sapiens. Human. Organism_taxid: 9606
Resolution:
2.60Å     R-factor:   0.226     R-free:   0.234
Authors: X.Ren,J.H.Hurley
Key ref: X.Ren and J.H.Hurley (2010). VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargo. Embo J, 29, 1045-1054. PubMed id: 20150893
Date:
13-Jan-10     Release date:   02-Mar-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		685 a.a.
73 a.a.
Protein chains
Pfam   ArchSchema ?
Q92783  (STAM1_HUMAN) -  Signal transducing adapter molecule 1 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		540 a.a.
140 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains F, A, D, B, C, E, G: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Embo J 29:1045-1054 (2010)
PubMed id: 20150893  
 
 
VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargo.
X.Ren, J.H.Hurley.
 
  ABSTRACT  
 
VHS (Vps27, Hrs, and STAM) domains occur in ESCRT-0 subunits Hrs and STAM, GGA adapters, and other trafficking proteins. The structure of the STAM VHS domain-ubiquitin complex was solved at 2.6 A resolution, revealing that determinants for ubiquitin recognition are conserved in nearly all VHS domains. VHS domains from all classes of VHS-domain containing proteins in yeast and humans, including both subunits of ESCRT-0, bound ubiquitin in vitro. ESCRTs have been implicated in the sorting of Lys63-linked polyubiquitinated cargo. Intact human ESCRT-0 binds Lys63-linked tetraubiquitin 50-fold more tightly than monoubiquitin, though only 2-fold more tightly than Lys48-linked tetraubiquitin. The gain in affinity is attributed to the cooperation of flexibly connected VHS and UIM motifs of ESCRT-0 in avid binding to the polyubiquitin chain. Mutational analysis of all the five ubiquitin-binding sites in yeast ESCRT-0 shows that cooperation between them is required for the sorting of the Lys63-linked polyubiquitinated cargo Cps1 to the vacuole.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22466610 Y.Nakazawa, K.Sasaki, N.Mitsutake, M.Matsuse, M.Shimada, T.Nardo, Y.Takahashi, K.Ohyama, K.Ito, H.Mishima, M.Nomura, A.Kinoshita, S.Ono, K.Takenaka, R.Masuyama, T.Kudo, H.Slor, A.Utani, S.Tateishi, S.Yamashita, M.Stefanini, A.R.Lehmann, K.Yoshiura, and T.Ogi (2012).
Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair.
  Nat Genet, 44, 586-592.  
21242292 D.K.Stringer, and R.C.Piper (2011).
A single ubiquitin is sufficient for cargo protein entry into MVBs in the absence of ESCRT ubiquitination.
  J Cell Biol, 192, 229-242.  
21332354 J.H.Hurley, and H.Stenmark (2011).
Molecular mechanisms of ubiquitin-dependent membrane traffic.
  Annu Rev Biophys, 40, 119-142.  
20927613 J.Lim, Y.H.Hong, B.J.Lee, and H.C.Ahn (2011).
Backbone (1)H, (13)C, and (15)N assignments for the tandem ubiquitin binding domains of signal transducing adapter molecule 1.
  Biomol NMR Assign, 5, 51-54.  
21030261 S.Peel, P.Macheboeuf, N.Martinelli, and W.Weissenhorn (2011).
Divergent pathways lead to ESCRT-III-catalyzed membrane fission.
  Trends Biochem Sci, 36, 199-210.  
20801936 H.Takai, Y.Xie, T.de Lange, and N.P.Pavletich (2010).
Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes.
  Genes Dev, 24, 2019-2030.
PDB code: 3o4z
  20653365 J.H.Hurley (2010).
The ESCRT complexes.
  Crit Rev Biochem Mol Biol, 45, 463-487.  
21145455 J.H.Hurley, E.Boura, L.A.Carlson, and B.Różycki (2010).
Membrane budding.
  Cell, 143, 875-887.  
21111229 M.J.Clague, and S.Urbé (2010).
Ubiquitin: same molecule, different degradation pathways.
  Cell, 143, 682-685.  
20975941 M.Zhadina, and P.D.Bieniasz (2010).
Functional interchangeability of late domains, late domain cofactors and ubiquitin in viral budding.
  PLoS Pathog, 6, e1001153.  
21070969 N.Pashkova, L.Gakhar, S.C.Winistorfer, L.Yu, S.Ramaswamy, and R.C.Piper (2010).
WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins.
  Mol Cell, 40, 433-443.
PDB code: 3odt
20974815 P.M.Apaja, H.Xu, and G.L.Lukacs (2010).
Quality control for unfolded proteins at the plasma membrane.
  J Cell Biol, 191, 553-570.  
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.

 

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