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PDBsum entry 2c5k

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protein ligands Protein-protein interface(s) links
Protein transport PDB id
2c5k

 

 

 

 

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Contents
Protein chains
22 a.a.
89 a.a.
Ligands
SO4 ×4
Waters ×114
PDB id:
2c5k
Name: Protein transport
Title: N-terminal domain of tlg1 complexed with n-terminus of vps51
Structure: Vacuolar protein sorting protein 51. Chain: p. Fragment: n-terminal residues 9-32. Synonym: vps51, apical bud growth protein 3. Engineered: yes. T-snare affecting a late golgi compartment protein 1. Chain: t. Fragment: n-terminal domain, residues 1-95. Synonym: syntaxin tlg1.
Source: Synthetic: yes. Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Biol. unit: Dimer (from PDB file)
Resolution:
2.05Å     R-factor:   0.177     R-free:   0.221
Authors: Y.Fridmann-Sirkis,H.M.Kent,M.J.Lewis,P.R.Evans,H.R.B.Pelham
Key ref: Y.Fridmann-Sirkis et al. (2006). Structural analysis of the interaction between the SNARE Tlg1 and Vps51. Traffic, 7, 182-190. PubMed id: 16420526
Date:
27-Oct-05     Release date:   25-Jan-06    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P36116  (VPS51_YEAST) -  Vacuolar protein sorting-associated protein 51 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
164 a.a.
22 a.a.
Protein chain
Pfam   ArchSchema ?
Q03322  (TLG1_YEAST) -  t-SNARE affecting a late Golgi compartment protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
224 a.a.
89 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Traffic 7:182-190 (2006)
PubMed id: 16420526  
 
 
Structural analysis of the interaction between the SNARE Tlg1 and Vps51.
Y.Fridmann-Sirkis, H.M.Kent, M.J.Lewis, P.R.Evans, H.R.Pelham.
 
  ABSTRACT  
 
Membrane fusion in cells involves the interaction of SNARE proteins on apposing membranes. Formation of SNARE complexes is preceded by tethering events, and a number of protein complexes that are thought to mediate this have been identified. The VFT or GARP complex is required for endosome-Golgi traffic in yeast. It consists of four subunits, one of which, Vps51, has been shown to bind specifically to the SNARE Tlg1, which participates in the same fusion event. We have determined the structure of the N-terminal domain of Tlg1 bound to a peptide from the N terminus of Vps51. Binding depends mainly on residues 18-30 of Vps51. These form a short helix which lies in a conserved groove in the three-helix bundle formed by Tlg1. Surprisingly, although both Vps51 and Tlg1 are required for transport to the late Golgi from endosomes, removal of the Tlg1-binding sequences from Vps51 does not block such traffic in vivo. Thus, this particular interaction cannot be crucial to the process of vesicle docking or fusion.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21183348 J.S.Bonifacino, and A.Hierro (2011).
Transport according to GARP: receiving retrograde cargo at the trans-Golgi network.
  Trends Cell Biol, 21, 159-167.  
21056839 C.Bröcker, S.Engelbrecht-Vandré, and C.Ungermann (2010).
Multisubunit tethering complexes and their role in membrane fusion.
  Curr Biol, 20, R943-R952.  
20685960 F.J.Pérez-Victoria, C.Schindler, J.G.Magadán, G.A.Mardones, C.Delevoye, M.Romao, G.Raposo, and J.S.Bonifacino (2010).
Ang2/fat-free is a conserved subunit of the Golgi-associated retrograde protein complex.
  Mol Biol Cell, 21, 3386-3395.  
20658963 J.Zimmermann, S.Chidambaram, and G.Fischer von Mollard (2010).
Dissecting Ent3p: the ENTH domain binds different SNAREs via distinct amino acid residues while the C-terminus is sufficient for retrograde transport from endosomes.
  Biochem J, 431, 123-134.  
19620288 F.J.Pérez-Victoria, and J.S.Bonifacino (2009).
Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-golgi network.
  Mol Cell Biol, 29, 5251-5263.  
19387489 M.Theis, M.Slabicki, M.Junqueira, M.Paszkowski-Rogacz, J.Sontheimer, R.Kittler, A.K.Heninger, T.Glatter, K.Kruusmaa, I.Poser, A.A.Hyman, M.T.Pisabarro, M.Gstaiger, R.Aebersold, A.Shevchenko, and F.Buchholz (2009).
Comparative profiling identifies C13orf3 as a component of the Ska complex required for mammalian cell division.
  EMBO J, 28, 1453-1465.  
18257909 C.Yanay, N.Morpurgo, and M.Linial (2008).
Evolution of insect proteomes: insights into synapse organization and synaptic vesicle life cycle.
  Genome Biol, 9, R27.  
18353293 R.D.Smith, and V.V.Lupashin (2008).
Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation.
  Carbohydr Res, 343, 2024-2031.  
18086915 A.Shestakova, E.Suvorova, O.Pavliv, G.Khaidakova, and V.Lupashin (2007).
Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability.
  J Cell Biol, 179, 1179-1192.  
17997821 D.Swennen, and J.M.Beckerich (2007).
Yarrowia lipolytica vesicle-mediated protein transport pathways.
  BMC Evol Biol, 7, 219.  
18074396 R.L.Rich, and D.G.Myszka (2007).
Survey of the year 2006 commercial optical biosensor literature.
  J Mol Recognit, 20, 300-366.  
18033301 S.E.Miller, B.M.Collins, A.J.McCoy, M.S.Robinson, and D.J.Owen (2007).
A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles.
  Nature, 450, 570-574.
PDB codes: 2qy7 2qyw 2v8s
17596510 T.H.Kloepper, C.N.Kienle, and D.Fasshauer (2007).
An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system.
  Mol Biol Cell, 18, 3463-3471.  
17319956 V.L.Koumandou, J.B.Dacks, R.M.Coulson, and M.C.Field (2007).
Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins.
  BMC Evol Biol, 7, 29.  
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 codes are shown on the right.

 

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