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PDBsum entry 2pfv

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Endocytosis/exocytosis PDB id
2pfv

 

 

 

 

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Contents
Protein chain
549 a.a. *
Waters ×111
* Residue conservation analysis
PDB id:
2pfv
Name: Endocytosis/exocytosis
Title: S. Cerevisiae exo70 with additional residues to 2.1 angrstrom resolution
Structure: Exocyst complex component exo70. Chain: a. Fragment: residues 62-623. Synonym: exocyst complex protein of 70 kda. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: exo70. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.237     R-free:   0.263
Authors: B.A.Moore,H.H.Robinson,Z.Xu
Key ref:
B.A.Moore et al. (2007). The crystal structure of mouse Exo70 reveals unique features of the mammalian exocyst. J Mol Biol, 371, 410-421. PubMed id: 17583731 DOI: 10.1016/j.jmb.2007.05.018
Date:
05-Apr-07     Release date:   22-May-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P19658  (EXO70_YEAST) -  Exocyst complex component EXO70 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
623 a.a.
549 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.jmb.2007.05.018 J Mol Biol 371:410-421 (2007)
PubMed id: 17583731  
 
 
The crystal structure of mouse Exo70 reveals unique features of the mammalian exocyst.
B.A.Moore, H.H.Robinson, Z.Xu.
 
  ABSTRACT  
 
The exocyst is a eukaryotic tethering complex necessary for the fusion of exocytic vesicles with the plasma membrane. Its function in vivo is tightly regulated by interactions with multiple small GTPases. Exo70, one of the eight subunits of the exocyst, is important for the localization of the exocyst to the plasma membrane. It interacts with TC10 and Rho3 GTPases in mammals and yeast, respectively, and has been shown recently to bind to the actin-polymerization complex Arp2/3. Here, we present the crystal structure of Mus musculus Exo70 at 2.25 A resolution. Exo70 is composed of alpha-helices in a series of right-handed helix-turn-helix motifs organized into a long rod of length 170 A and width 35 A. Although the alpha-helical organization of this molecule is similar to that in Saccharomyces cerevisiae Exo70, major structural differences are observed on the surface of the molecule, at the domain boundaries, and in various loop structures. In particular, the C-terminal domain of M. musculus Exo70 adopts a new orientation relative to the N-terminal half not seen in S. cerevisiae Exo70 structures. Given the low level of sequence conservation within Exo70, this structure provides new insights into our understanding of many species-specific functions of the exocyst.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. A stereo cartoon diagram of MmExo70 is shown. Residues are shown in color: N domain, red; M domain, yellow; and C domain, blue. The α-helices are drawn as coils and labeled from H1 to H19; turns and loops, solid tubes; unobserved residues, broken lines (no β strands are observed in the structure).
Figure 2.
Figure 2. Structural alignment of Exo70 in M. musculus, H. sapiens, D. melanogaster, S. pombe, and S. cerevisiae. Invariant residues are shaded purple. Similar but not identical residues are shaded pink. Secondary structural elements are indicated above the sequence block for MmExo70 and below for ScExo70: α-helices, rectangles; other elements, continuous lines; structurally unobserved residues, broken lines. For MmExo70: N domain, red; M domain, yellow; and C domain, blue (same as Figure 1). For ScExo70: N domain, brown; M domain, green; and C domain, cyan. For clarity, sequences lacking homology or unobserved in the structures have been replaced with bracketed numbers indicating the number of residues omitted.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2007, 371, 410-421) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21235523 M.Hertzog, and P.Chavrier (2011).
Cell polarity during motile processes: keeping on track with the exocyst complex.
  Biochem J, 433, 403-409.  
21145407 S.Ory, and S.Gasman (2011).
Rho GTPases and exocytosis: what are the molecular links?
  Semin Cell Dev Biol, 22, 27-32.  
20615984 F.J.Pérez-Victoria, G.Abascal-Palacios, I.Tascón, A.Kajava, J.G.Magadán, E.P.Pioro, J.S.Bonifacino, and A.Hierro (2010).
Structural basis for the wobbler mouse neurodegenerative disorder caused by mutation in the Vps54 subunit of the GARP complex.
  Proc Natl Acad Sci U S A, 107, 12860-12865.
PDB codes: 3n1b 3n1e
19955214 H.Wu, C.Turner, J.Gardner, B.Temple, and P.Brennwald (2010).
The Exo70 subunit of the exocyst is an effector for both Cdc42 and Rho3 function in polarized exocytosis.
  Mol Biol Cell, 21, 430-442.  
19575650 I.M.Yu, and F.M.Hughson (2010).
Tethering factors as organizers of intracellular vesicular traffic.
  Annu Rev Cell Dev Biol, 26, 137-156.  
20139078 K.Baek, A.Knödler, S.H.Lee, X.Zhang, K.Orlando, J.Zhang, T.J.Foskett, W.Guo, and R.Dominguez (2010).
Structure-function study of the N-terminal domain of exocyst subunit Sec3.
  J Biol Chem, 285, 10424-10433.
PDB code: 3hie
20062059 M.Yamashita, K.Kurokawa, Y.Sato, A.Yamagata, H.Mimura, A.Yoshikawa, K.Sato, A.Nakano, and S.Fukai (2010).
Structural basis for the Rho- and phosphoinositide-dependent localization of the exocyst subunit Sec3.
  Nat Struct Mol Biol, 17, 180-186.
PDB code: 3a58
18946089 A.H.Hutagalung, J.Coleman, M.Pypaert, and P.J.Novick (2009).
An internal domain of Exo70p is required for actin-independent localization and mediates assembly of specific exocyst components.
  Mol Biol Cell, 20, 153-163.  
19151722 A.Tripathi, Y.Ren, P.D.Jeffrey, and F.M.Hughson (2009).
Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex.
  Nat Struct Mol Biol, 16, 114-123.
PDB codes: 3etu 3etv 3fhn
19651599 B.C.Richardson, R.D.Smith, D.Ungar, A.Nakamura, P.D.Jeffrey, V.V.Lupashin, and F.M.Hughson (2009).
Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene.
  Proc Natl Acad Sci U S A, 106, 13329-13334.
PDB code: 3hr0
19473826 B.He, and W.Guo (2009).
The exocyst complex in polarized exocytosis.
  Curr Opin Cell Biol, 21, 537-542.  
19887069 E.Sztul, and V.Lupashin (2009).
Role of vesicle tethering factors in the ER-Golgi membrane traffic.
  FEBS Lett, 583, 3770-3783.  
20019791 H.Lu, L.Lin, S.Sato, Y.Xing, and C.J.Lee (2009).
Predicting functional alternative splicing by measuring RNA selection pressure from multigenome alignments.
  PLoS Comput Biol, 5, e1000608.  
19073882 J.A.Songer, and M.Munson (2009).
Sec6p anchors the assembled exocyst complex at sites of secretion.
  Mol Biol Cell, 20, 973-982.  
19214222 N.J.Croteau, M.L.Furgason, D.Devos, and M.Munson (2009).
Conservation of helical bundle structure between the exocyst subunits.
  PLoS ONE, 4, e4443.  
19552648 T.Hubert, J.Vandekerckhove, and J.Gettemans (2009).
Exo70-mediated recruitment of nucleoporin Nup62 at the leading edge of migrating cells is required for cell migration.
  Traffic, 10, 1257-1271.  
20005805 Y.Ren, C.K.Yip, A.Tripathi, D.Huie, P.D.Jeffrey, T.Walz, and F.M.Hughson (2009).
A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1.
  Cell, 139, 1119-1129.
PDB code: 3k8p
18480549 T.Saito, T.Shibasaki, and S.Seino (2008).
Involvement of Exoc3l, a protein structurally related to the exocyst subunit Sec6, in insulin secretion.
  Biomed Res, 29, 85-91.  
17761530 J.Liu, X.Zuo, P.Yue, and W.Guo (2007).
Phosphatidylinositol 4,5-bisphosphate mediates the targeting of the exocyst to the plasma membrane for exocytosis in mammalian cells.
  Mol Biol Cell, 18, 4483-4492.  
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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