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Protein binding PDB id
1nz6
Jmol
Contents
Protein chains
98 a.a. *
Waters ×21
* Residue conservation analysis
PDB id:
1nz6
Name: Protein binding
Title: Crystal structure of auxilin j-domain
Structure: Auxilin. Chain: a, b. Fragment: j-domain. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Tissue: brain. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.234     R-free:   0.268
Authors: J.Jiang,A.B.Taylor,K.Prasad,Y.Ishikawa-Brush,P.J.Hart,E.M.La R.Sousa
Key ref:
J.Jiang et al. (2003). Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface. Biochemistry, 42, 5748-5753. PubMed id: 12741832 DOI: 10.1021/bi034270g
Date:
16-Feb-03     Release date:   22-Apr-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q27974  (AUXI_BOVIN) -  Putative tyrosine-protein phosphatase auxilin
Seq:
Struc: 		 
Seq:
Struc: 		910 a.a.
98 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
 + H(2)O
 = protein tyrosine
 + phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     heat shock protein binding     1 term  

 

 
    reference    
 
 
DOI no: 10.1021/bi034270g Biochemistry 42:5748-5753 (2003)
PubMed id: 12741832  
 
 
Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface.
J.Jiang, A.B.Taylor, K.Prasad, Y.Ishikawa-Brush, P.J.Hart, E.M.Lafer, R.Sousa.
 
  ABSTRACT  
 
J-domains are widespread protein interaction modules involved in recruiting and stimulating the activity of Hsp70 family chaperones. We have determined the crystal structure of the J-domain of auxilin, a protein which is involved in uncoating clathrin-coated vesicles. Comparison to the known structures of J-domains from four other proteins reveals that the auxilin J-domain is the most divergent of all J-domain structures described to date. In addition to the canonical J-domain features described previously, the auxilin J-domain contains an extra N-terminal helix and a long loop inserted between helices I and II. The latter loop extends the positively charged surface which forms the Hsc70 binding site, and is shown by directed mutagenesis and surface plasmon resonance to contain side chains important for binding to Hsc70.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21329881 M.Hagiwara, K.Maegawa, M.Suzuki, R.Ushioda, K.Araki, Y.Matsumoto, J.Hoseki, K.Nagata, and K.Inaba (2011).
Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5.
  Mol Cell, 41, 432-444.
PDB codes: 3apo 3apq 3aps
20562448 A.Takano, N.Suetsugu, M.Wada, and D.Kohda (2010).
Crystallographic and functional analyses of J-domain of JAC1 essential for chloroplast photorelocation movement in Arabidopsis thaliana.
  Plant Cell Physiol, 51, 1372-1376.
PDB code: 3ag7
19519518 J.Li, X.Qian, and B.Sha (2009).
Heat shock protein 40: structural studies and their functional implications.
  Protein Pept Lett, 16, 606-612.  
17984091 S.P.Acebrón, V.Fernández-Sáiz, S.G.Taneva, F.Moro, and A.Muga (2008).
DnaJ recruits DnaK to protein aggregates.
  J Biol Chem, 283, 1381-1390.  
17488288 E.Eisenberg, and L.E.Greene (2007).
Multiple roles of auxilin and hsc70 in clathrin-mediated endocytosis.
  Traffic, 8, 640-646.  
17996706 J.Jiang, E.G.Maes, A.B.Taylor, L.Wang, A.P.Hinck, E.M.Lafer, and R.Sousa (2007).
Structural basis of J cochaperone binding and regulation of Hsp70.
  Mol Cell, 28, 422-433.
PDB codes: 2qw9 2qwl 2qwm 2qwn 2qwo 2qwp 2qwq 2qwr
17239655 W.S.Nicoll, M.Botha, C.McNamara, M.Schlange, E.R.Pesce, A.Boshoff, M.H.Ludewig, R.Zimmermann, M.E.Cheetham, J.P.Chapple, and G.L.Blatch (2007).
Cytosolic and ER J-domains of mammalian and parasitic origin can functionally interact with DnaK.
  Int J Biochem Cell Biol, 39, 736-751.  
16798879 R.H.Massol, W.Boll, A.M.Griffin, and T.Kirchhausen (2006).
A burst of auxilin recruitment determines the onset of clathrin-coated vesicle uncoating.
  Proc Natl Acad Sci U S A, 103, 10265-10270.  
17026666 R.Sousa, and E.M.Lafer (2006).
Keep the traffic moving: mechanism of the Hsp70 motor.
  Traffic, 7, 1596-1603.  
15987899 F.Hennessy, W.S.Nicoll, R.Zimmermann, M.E.Cheetham, and G.L.Blatch (2005).
Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions.
  Protein Sci, 14, 1697-1709.  
16307916 J.Jiang, K.Prasad, E.M.Lafer, and R.Sousa (2005).
Structural basis of interdomain communication in the Hsc70 chaperone.
  Mol Cell, 20, 513-524.
PDB code: 1yuw
15549676 R.L.Rich, and D.G.Myszka (2005).
Survey of the year 2003 commercial optical biosensor literature.
  J Mol Recognit, 18, 1.  
15502813 A.Fotin, Y.Cheng, N.Grigorieff, T.Walz, S.C.Harrison, and T.Kirchhausen (2004).
Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating.
  Nature, 432, 649-653.
PDB code: 1xi5
15273304 J.M.Gruschus, L.E.Greene, E.Eisenberg, and J.A.Ferretti (2004).
Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural change.
  Protein Sci, 13, 2029-2044.  
15170475 P.Walsh, D.Bursać, Y.C.Law, D.Cyr, and T.Lithgow (2004).
The J-protein family: modulating protein assembly, disassembly and translocation.
  EMBO Rep, 5, 567-571.  
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.