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PDBsum entry 1f6b

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protein ligands metals Protein-protein interface(s) links
Protein transport PDB id
1f6b

 

 

 

 

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Contents
Protein chains
176 a.a. *
Ligands
SO4 ×5
GDP ×2
Metals
_MG ×2
Waters ×297
* Residue conservation analysis
PDB id:
1f6b
Name: Protein transport
Title: Crystal structure of sar1-gdp complex
Structure: Sar1. Chain: a, b. Engineered: yes
Source: Cricetulus griseus. Chinese hamster. Organism_taxid: 10029. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
1.70Å     R-factor:   0.220     R-free:   0.240
Authors: M.Huang,I.A.Wilson,W.E.Balch
Key ref: M.Huang et al. (2001). Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export. J Cell Biol, 155, 937-948. PubMed id: 11739406
Date:
21-Jun-00     Release date:   09-Jan-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9QVY3  (SAR1B_CRIGR) -  GTP-binding protein SAR1b from Cricetulus griseus
Seq:
Struc:
198 a.a.
176 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
J Cell Biol 155:937-948 (2001)
PubMed id: 11739406  
 
 
Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export.
M.Huang, J.T.Weissman, S.Beraud-Dufour, P.Luan, C.Wang, W.Chen, M.Aridor, I.A.Wilson, W.E.Balch.
 
  ABSTRACT  
 
The Sar1 GTPase is an essential component of COPII vesicle coats involved in export of cargo from the ER. We report the 1.7-A structure of Sar1 and find that consistent with the sequence divergence of Sar1 from Arf family GTPases, Sar1 is structurally distinct. In particular, we show that the Sar1 NH2 terminus contains two regions: an NH2-terminal extension containing an evolutionary conserved hydrophobic motif that facilitates membrane recruitment and activation by the mammalian Sec12 guanine nucleotide exchange factor, and an alpha1' amphipathic helix that contributes to interaction with the Sec23/24 complex that is responsible for cargo selection during ER export. We propose that the hydrophobic Sar1 NH2-terminal activation/recruitment motif, in conjunction with the alpha1' helix, mediates the initial steps in COPII coat assembly for export from the ER.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22193160 G.Zanetti, K.B.Pahuja, S.Studer, S.Shim, and R.Schekman (2012).
COPII and the regulation of protein sorting in mammals.
  Nat Cell Biol, 14, 20-28.  
21291503 C.Kodera, T.Yorimitsu, A.Nakano, and K.Sato (2011).
Sed4p stimulates Sar1p GTP hydrolysis and promotes limited coat disassembly.
  Traffic, 12, 591-599.  
20624903 K.R.Long, Y.Yamamoto, A.L.Baker, S.C.Watkins, C.B.Coyne, J.F.Conway, and M.Aridor (2010).
Sar1 assembly regulates membrane constriction and ER export.
  J Cell Biol, 190, 115-128.  
19763084 K.V.Tabata, K.Sato, T.Ide, T.Nishizaka, A.Nakano, and H.Noji (2009).
Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane.
  EMBO J, 28, 3279-3289.  
19188365 S.Susuki, T.Sato, M.Miyata, M.Momohara, M.A.Suico, T.Shuto, Y.Ando, and H.Kai (2009).
The Endoplasmic Reticulum-associated Degradation of Transthyretin Variants Is Negatively Regulated by BiP in Mammalian Cells.
  J Biol Chem, 284, 8312-8321.  
19368893 T.Zhang, S.Li, Y.Zhang, C.Zhong, Z.Lai, and J.Ding (2009).
Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector.
  Structure, 17, 602-610.
PDB codes: 3doe 3dof
  19052367 E.H.Jang, H.Park, A.K.Park, J.H.Moon, Y.M.Chi, and I.Y.Ahn (2008).
Crystallization and preliminary X-ray crystallographic studies of the rho-class glutathione S-transferase from the Antarctic clam Laternula elliptica.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1132-1134.  
18060556 H.Hughes, and D.J.Stephens (2008).
Assembly, organization, and function of the COPII coat.
  Histochem Cell Biol, 129, 129-151.  
18322804 S.L.Hanton, L.Chatre, L.A.Matheson, M.Rossi, M.A.Held, and F.Brandizzi (2008).
Plant Sar1 isoforms with near-identical protein sequences exhibit different localisations and effects on secretion.
  Plant Mol Biol, 67, 283-294.  
17686639 M.C.Lee, and E.A.Miller (2007).
Molecular mechanisms of COPII vesicle formation.
  Semin Cell Dev Biol, 18, 424-434.  
17395454 S.M.Stagg, P.LaPointe, and W.E.Balch (2007).
Structural design of cage and coat scaffolds that direct membrane traffic.
  Curr Opin Struct Biol, 17, 221-228.  
16990852 C.Gürkan, S.M.Stagg, P.Lapointe, and W.E.Balch (2006).
The COPII cage: unifying principles of vesicle coat assembly.
  Nat Rev Mol Cell Biol, 7, 727-738.  
16505163 R.A.Kahn, J.Cherfils, M.Elias, R.C.Lovering, S.Munro, and A.Schurmann (2006).
Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins.
  J Cell Biol, 172, 645-650.  
16344311 A.Bielli, C.J.Haney, G.Gabreski, S.C.Watkins, S.I.Bannykh, and M.Aridor (2005).
Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission.
  J Cell Biol, 171, 919-924.  
15985540 D.C.Tang, J.Zhu, W.Liu, K.Chin, J.Sun, L.Chen, J.A.Hanover, and G.P.Rodgers (2005).
The hydroxyurea-induced small GTP-binding protein SAR modulates gamma-globin gene expression in human erythroid cells.
  Blood, 106, 3256-3263.  
15752134 J.D.Mancias, and J.Goldberg (2005).
Exiting the endoplasmic reticulum.
  Traffic, 6, 278-285.  
16122427 M.C.Lee, L.Orci, S.Hamamoto, E.Futai, M.Ravazzola, and R.Schekman (2005).
Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle.
  Cell, 122, 605-617.  
15891388 M.M.Hussain, S.Fatma, X.Pan, and J.Iqbal (2005).
Intestinal lipoprotein assembly.
  Curr Opin Lipidol, 16, 281-285.  
15752133 S.L.Hanton, L.E.Bortolotti, L.Renna, G.Stefano, and F.Brandizzi (2005).
Crossing the divide--transport between the endoplasmic reticulum and Golgi apparatus in plants.
  Traffic, 6, 267-277.  
14978301 C.Blouin, D.Butt, and A.J.Roger (2004).
Rapid evolution in conformational space: a study of loop regions in a ubiquitous GTP binding domain.
  Protein Sci, 13, 608-616.  
15017362 C.C.Shoulders, D.J.Stephens, and B.Jones (2004).
The intracellular transport of chylomicrons requires the small GTPase, Sar1b.
  Curr Opin Lipidol, 15, 191-197.  
15564045 C.G.Burd, T.I.Strochlic, and S.R.Gangi Setty (2004).
Arf-like GTPases: not so Arf-like after all.
  Trends Cell Biol, 14, 687-694.  
15093828 L.C.Bickford, E.Mossessova, and J.Goldberg (2004).
A structural view of the COPII vesicle coat.
  Curr Opin Struct Biol, 14, 147-153.  
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.  
15149587 P.LaPointe, C.Gurkan, and W.E.Balch (2004).
Mise en place-this bud's for the Golgi.
  Mol Cell, 14, 413-414.  
15479737 X.Wang, J.Matteson, Y.An, B.Moyer, J.S.Yoo, S.Bannykh, I.A.Wilson, J.R.Riordan, and W.E.Balch (2004).
COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code.
  J Cell Biol, 167, 65-74.  
12692552 B.Jones, E.L.Jones, S.A.Bonney, H.N.Patel, A.R.Mensenkamp, S.Eichenbaum-Voline, M.Rudling, U.Myrdal, G.Annesi, S.Naik, N.Meadows, A.Quattrone, S.A.Islam, R.P.Naoumova, B.Angelin, R.Infante, E.Levy, C.C.Roy, P.S.Freemont, J.Scott, and C.C.Shoulders (2003).
Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders.
  Nat Genet, 34, 29-31.  
12972562 C.G.Giraudo, and H.J.Maccioni (2003).
Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1.
  Mol Biol Cell, 14, 3753-3766.  
14579253 G.Jékely (2003).
Small GTPases and the evolution of the eukaryotic cell.
  Bioessays, 25, 1129-1138.  
12383791 C.Barlowe (2002).
COPII-dependent transport from the endoplasmic reticulum.
  Curr Opin Cell Biol, 14, 417-422.  
12429613 S.Pasqualato, L.Renault, and J.Cherfils (2002).
Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication.
  EMBO Rep, 3, 1035-1041.  
12239560 X.Bi, R.A.Corpina, and J.Goldberg (2002).
Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat.
  Nature, 419, 271-277.
PDB codes: 1m2o 1m2v
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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