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PDBsum entry 3haj
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protein metals Protein-protein interface(s) links
Endocytosis PDB id
3haj

 

 

 

 

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Contents
Protein chains
286 a.a. *
Metals
_CA ×2
Waters ×36
* Residue conservation analysis
PDB id:
3haj
Name: Endocytosis
Title: Crystal structure of human pacsin2 f-bar domain (p212121 lattice)
Structure: Human pacsin2 f-bar. Chain: a, b. Synonym: protein kinasE C and casein kinase substrate in neurons protein 2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pacsin2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.78Å     R-factor:   0.227     R-free:   0.274
Authors: Q.Wang,M.V.A.S.Navarro,G.Peng,K.R.Rajashankar,H.Sondermann
Key ref: Q.Wang et al. (2009). Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin. Proc Natl Acad Sci U S A, 106, 12700-12705. PubMed id: 19549836
Date:
01-May-09     Release date:   16-Jun-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9UNF0  (PACN2_HUMAN) -  Protein kinase C and casein kinase substrate in neurons protein 2 from Homo sapiens
Seq:
Struc: 		486 a.a.
286 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Proc Natl Acad Sci U S A 106:12700-12705 (2009)
PubMed id: 19549836  
 
 
Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin.
Q.Wang, M.V.Navarro, G.Peng, E.Molinelli, S.L.Goh, B.L.Judson, K.R.Rajashankar, H.Sondermann.
 
  ABSTRACT  
 
Peripheral membrane proteins of the Bin/amphiphysin/Rvs (BAR) and Fer-CIP4 homology-BAR (F-BAR) family participate in cellular membrane trafficking and have been shown to generate membrane tubules. The degree of membrane bending appears to be encoded in the structure and immanent curvature of the particular protein domains, with BAR and F-BAR domains inducing high- and low-curvature tubules, respectively. In addition, oligomerization and the formation of ordered arrays influences tubule stabilization. Here, the F-BAR domain-containing protein Pacsin was found to possess a unique activity, creating small tubules and tubule constrictions, in addition to the wide tubules characteristic for this subfamily. Based on crystal structures of the F-BAR domain of Pacsin and mutagenesis studies, vesiculation could be linked to the presence of unique structural features distinguishing it from other F-BAR proteins. Tubulation was suppressed in the context of the full-length protein, suggesting that Pacsin is autoinhibited in solution. The regulated deformation of membranes and promotion of tubule constrictions by Pacsin suggests a more versatile function of these proteins in vesiculation and endocytosis beyond their role as scaffold proteins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21549705 D.Ruffell (2011).
Featuring… Shiro Suetsugu Winner of the 2011 FEBS Letters Young Group Leader Award.
  FEBS Lett, 585, 1504-1505.  
21445324 M.J.Taylor, D.Perrais, and C.J.Merrifield (2011).
A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis.
  PLoS Biol, 9, e1000604.  
20837154 R.Ramachandran (2011).
Vesicle scission: dynamin.
  Semin Cell Dev Biol, 22, 10-17.  
21219150 T.Baumgart, B.R.Capraro, C.Zhu, and S.L.Das (2011).
Thermodynamics and mechanics of membrane curvature generation and sensing by proteins and lipids.
  Annu Rev Phys Chem, 62, 483-506.  
  20581461 G.A.Quiñones, and A.E.Oro (2010).
BAR domain competition during directional cellular migration.
  Cell Cycle, 9, 2522-2528.  
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.  
20300118 M.Lenoir, U.Coskun, M.Grzybek, X.Cao, S.B.Buschhorn, J.James, K.Simons, and M.Overduin (2010).
Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains.
  EMBO Rep, 11, 279-284.  
20083215 M.Masuda, and N.Mochizuki (2010).
Structural characteristics of BAR domain superfamily to sculpt the membrane.
  Semin Cell Dev Biol, 21, 391-398.  
20603077 R.H.Roberts-Galbraith, M.D.Ohi, B.A.Ballif, J.S.Chen, I.McLeod, W.H.McDonald, S.P.Gygi, J.R.Yates, and K.L.Gould (2010).
Dephosphorylation of F-BAR protein Cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site.
  Mol Cell, 39, 86-99.  
  20585502 S.Ahmed, W.Bu, R.T.Lee, S.Maurer-Stroh, and W.I.Goh (2010).
F-BAR domain proteins: Families and function.
  Commun Integr Biol, 3, 116-121.  
20435640 S.Suetsugu (2010).
The proposed functions of membrane curvatures mediated by the BAR domain superfamily proteins.
  J Biochem, 148, 1.  
19963073 S.Suetsugu, K.Toyooka, and Y.Senju (2010).
Subcellular membrane curvature mediated by the BAR domain superfamily proteins.
  Semin Cell Dev Biol, 21, 340-349.  
20467216 T.Takenawa (2010).
Phosphoinositide-binding interface proteins involved in shaping cell membranes.
  Proc Jpn Acad Ser B Phys Biol Sci, 86, 509-523.  
20404169 Y.Rao, Q.Ma, A.Vahedi-Faridi, A.Sundborger, A.Pechstein, D.Puchkov, L.Luo, O.Shupliakov, W.Saenger, and V.Haucke (2010).
Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation.
  Proc Natl Acad Sci U S A, 107, 8213-8218.
PDB codes: 2x3v 2x3w 2x3x
19713939 A.Reider, S.L.Barker, S.K.Mishra, Y.J.Im, L.Maldonado-Báez, J.H.Hurley, L.M.Traub, and B.Wendland (2009).
Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation.
  EMBO J, 28, 3103-3116.
PDB codes: 3g9g 3g9h
19997509 M.A.Edeling, S.Sanker, T.Shima, P.K.Umasankar, S.Höning, H.Y.Kim, L.A.Davidson, S.C.Watkins, M.Tsang, D.J.Owen, and L.M.Traub (2009).
Structural requirements for PACSIN/Syndapin operation during zebrafish embryonic notochord development.
  PLoS One, 4, e8150.
PDB code: 3i2w
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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