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PDBsum entry 1r4x
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protein metals links
Protein transport PDB id
1r4x

 

 

 

 

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Contents
Protein chain
274 a.a. *
Metals
_MG
Waters ×254
* Residue conservation analysis
PDB id:
1r4x
Name: Protein transport
Title: Crystal structure analys of the gamma-copi appendage domain
Structure: Coatomer gamma subunit. Chain: a. Synonym: gamma1-cop. Coatomer protein complex, subunit gamma 1. Coat protein gamma-cop. Gamma-coat protein. Gamma-cop. Coat protein gamma- cop. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.175     R-free:   0.208
Authors: P.J.Watson,G.Frigerio,B.M.Collins,R.Duden,D.J.Owen
Key ref: P.J.Watson et al. (2004). Gamma-COP appendage domain - structure and function. Traffic, 5, 79-88. PubMed id: 14690497
Date:
09-Oct-03     Release date:   28-Oct-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9Y678  (COPG1_HUMAN) -  Coatomer subunit gamma-1 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		874 a.a.
274 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 9 residue positions (black crosses)

 

 
Traffic 5:79-88 (2004)
PubMed id: 14690497  
 
 
Gamma-COP appendage domain - structure and function.
P.J.Watson, G.Frigerio, B.M.Collins, R.Duden, D.J.Owen.
 
  ABSTRACT  
 
COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The cytosolic precursor of the COPI coat, the heptameric coatomer complex, can be thought of as composed of two subcomplexes. The first consists of the beta-, gamma-, delta- and zeta-COP subunits which are distantly homologous to AP clathrin adaptor subunits. The second consists of the alpha-, beta'- and epsilon-COP subunits. Here, we present the structure of the appendage domain of gamma-COP and show that it has a similar overall fold as the alpha-appendage of AP2. Again, like the alpha-appendage the gamma-COP appendage possesses a single protein/protein interaction site on its platform subdomain. We show that in yeast this site binds to the ARFGAP Glo3p, and in mammalian gamma-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP appendage that interacts with the alpha,beta',epsilon COPI subcomplex.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20534429 K.C.Hsia, and A.Hoelz (2010).
Crystal structure of alpha-COP in complex with epsilon-COP provides insight into the architecture of the COPI vesicular coat.
  Proc Natl Acad Sci U S A, 107, 11271-11276.
PDB codes: 3mv2 3mv3
19299515 A.Saitoh, H.W.Shin, A.Yamada, S.Waguri, and K.Nakayama (2009).
Three Homologous ArfGAPs Participate in Coat Protein I-mediated Transport.
  J Biol Chem, 284, 13948-13957.  
19109418 L.Kliouchnikov, J.Bigay, B.Mesmin, A.Parnis, M.Rawet, N.Goldfeder, B.Antonny, and D.Cassel (2009).
Discrete determinants in ArfGAP2/3 conferring Golgi localization and regulation by the COPI coat.
  Mol Biol Cell, 20, 859-869.  
19039328 Y.Deng, M.P.Golinelli-Cohen, E.Smirnova, and C.L.Jackson (2009).
A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor.
  EMBO Rep, 10, 58-64.  
18211691 C.J.DeRegis, P.B.Rahl, G.R.Hoffman, R.A.Cerione, and R.N.Collins (2008).
Mutational analysis of betaCOP (Sec26p) identifies an appendage domain critical for function.
  BMC Cell Biol, 9, 3.  
19015319 C.Weimer, R.Beck, P.Eckert, I.Reckmann, J.Moelleken, B.Brügger, and F.Wieland (2008).
Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking.
  J Cell Biol, 183, 725-735.  
18809720 R.A.Kahn, E.Bruford, H.Inoue, J.M.Logsdon, Z.Nie, R.T.Premont, P.A.Randazzo, M.Satake, A.B.Theibert, M.L.Zapp, and D.Cassel (2008).
Consensus nomenclature for the human ArfGAP domain-containing proteins.
  J Cell Biol, 182, 1039-1044.  
18434597 Y.Guo, V.Punj, D.Sengupta, and A.D.Linstedt (2008).
Coat-tether interaction in Golgi organization.
  Mol Biol Cell, 19, 2830-2843.  
17506703 A.K.Gillingham, and S.Munro (2007).
The small G proteins of the Arf family and their regulators.
  Annu Rev Cell Dev Biol, 23, 579-611.  
17760859 G.Frigerio, N.Grimsey, M.Dale, I.Majoul, and R.Duden (2007).
Two human ARFGAPs associated with COP-I-coated vesicles.
  Traffic, 8, 1644-1655.  
17666108 H.Inoue, and P.A.Randazzo (2007).
Arf GAPs and their interacting proteins.
  Traffic, 8, 1465-1475.  
17360540 J.Moelleken, J.Malsam, M.J.Betts, A.Movafeghi, I.Reckmann, I.Meissner, A.Hellwig, R.B.Russell, T.Söllner, B.Brügger, and F.T.Wieland (2007).
Differential localization of coatomer complex isoforms within the Golgi apparatus.
  Proc Natl Acad Sci U S A, 104, 4425-4430.  
17451557 Z.Sun, F.Anderl, K.Fröhlich, L.Zhao, S.Hanke, B.Brügger, F.Wieland, and J.Béthune (2007).
Multiple and stepwise interactions between coatomer and ADP-ribosylation factor-1 (Arf1)-GTP.
  Traffic, 8, 582-593.  
16316994 A.Parnis, M.Rawet, L.Regev, B.Barkan, M.Rotman, M.Gaitner, and D.Cassel (2006).
Golgi localization determinants in ArfGAP1 and in new tissue-specific ArfGAP1 isoforms.
  J Biol Chem, 281, 3785-3792.  
17041781 J.Béthune, F.Wieland, and J.Moelleken (2006).
COPI-mediated transport.
  J Membr Biol, 211, 65-79.  
16940185 J.Béthune, M.Kol, J.Hoffmann, I.Reckmann, B.Brügger, and F.Wieland (2006).
Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins.
  Mol Cell Biol, 26, 8011-8021.  
16493411 M.A.Edeling, C.Smith, and D.Owen (2006).
Life of a clathrin coat: insights from clathrin and AP structures.
  Nat Rev Mol Cell Biol, 7, 32-44.  
16476741 S.Hata, S.Koyama, H.Kawahara, N.Doi, T.Maeda, N.Toyama-Sorimachi, K.Abe, K.Suzuki, and H.Sorimachi (2006).
Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the beta-subunit of coatomer complex, beta-COP.
  J Biol Chem, 281, 11214-11224.  
16093346 D.M.Meyer, P.Crottet, B.Maco, E.Degtyar, D.Cassel, and M.Spiess (2005).
Oligomerization and dissociation of AP-1 adaptors are regulated by cargo signals and by ArfGAP1-induced GTP hydrolysis.
  Mol Biol Cell, 16, 4745-4754.  
15944734 J.Bigay, J.F.Casella, G.Drin, B.Mesmin, and B.Antonny (2005).
ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif.
  EMBO J, 24, 2244-2253.  
15473838 D.J.Owen, B.M.Collins, and P.R.Evans (2004).
Adaptors for clathrin coats: structure and function.
  Annu Rev Cell Dev Biol, 20, 153-191.  
15261670 H.T.McMahon, and I.G.Mills (2004).
COP and clathrin-coated vesicle budding: different pathways, common approaches.
  Curr Opin Cell Biol, 16, 379-391.  
15473836 M.C.Lee, E.A.Miller, J.Goldberg, L.Orci, and R.Schekman (2004).
Bi-directional protein transport between the ER and Golgi.
  Annu Rev Cell Dev Biol, 20, 87.  
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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