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Gene regulation PDB id
1dxs
Jmol
Contents
Protein chain
57 a.a. *
Waters ×26
* Residue conservation analysis
PDB id:
1dxs
Name: Gene regulation
Title: Crystal structure of thE C-terminal sterile alpha motif (sam) domain of human p73 alpha splice variant
Structure: P53-like transcription factor. Chain: a. Fragment: c-terminal sterile alpha motif (sam) domain. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: nucleus. Gene: p73. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.54Å     R-factor:   0.275     R-free:   0.346
Authors: W.K.Wang,Y.W.Chen
Key ref:
W.K.Wang et al. (2001). Structure of the C-terminal sterile alpha-motif (SAM) domain of human p73 alpha. Acta Crystallogr D Biol Crystallogr, 57, 545-551. PubMed id: 11264583 DOI: 10.1107/S0907444901002529
Date:
15-Jan-00     Release date:   12-Jan-01    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O15350  (P73_HUMAN) -  Tumor protein p73
Seq:
Struc: 		 
Seq:
Struc: 		636 a.a.
57 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1107/S0907444901002529 Acta Crystallogr D Biol Crystallogr 57:545-551 (2001)
PubMed id: 11264583  
 
 
Structure of the C-terminal sterile alpha-motif (SAM) domain of human p73 alpha.
W.K.Wang, M.Bycroft, N.W.Foster, A.M.Buckle, A.R.Fersht, Y.W.Chen.
 
  ABSTRACT  
 
p73 is a homologue of the tumour suppressor p53 and contains all three functional domains of p53. The alpha-splice variant of p73 (p73 alpha) contains near its C-terminus an additional structural domain known as the sterile alpha-motif (SAM) that is probably responsible for regulating p53-like functions of p73. Here, the 2.54 A resolution crystal structure of this protein domain is reported. The crystal structure and the published solution structure have the same five-helix bundle fold that is characteristic of all SAM-domain structures, with an overall r.m.s.d. of 1.5 A for main-chain atoms. The hydrophobic core residues are well conserved, yet some large local differences are observed. The crystal structure reveals a dimeric organization, with the interface residues forming a mini four-helix bundle. However, analysis of solvation free energies and the surface area buried upon dimer formation indicated that this arrangement is more likely to be an effect of crystal packing rather than reflecting a physiological state. This is consistent with the solution structure being a monomer. The p73 alpha SAM domain also contains several interesting structural features: a Cys-X-X-Cys motif, a 3(10)-helix and a loop that have elevated B factors, and short tight inter-helical loops including two beta-turns; these elements are probably important in the normal function of this domain.
 
  Selected figure(s)  
 
Figure 4.
Figure 4 The overall structure of p73 -SAM, coloured according to the fluctuations in crystallographic B factors. Colour code: spectrally from red, the highest B factors, to green, intermediate and blue, the lowest. 		Figure 5.
Figure 5 The potential CXXC motif in the p73 -SAM crystal structure. The 2mF[o] - DF[c]electron-density map covering Cys502-Pro503-Asn504-Cys505 contoured at 1.0 is shown. The CXXC motif of the oxidized disulfide-bond-formation protein DsbA (PDB code [248]1fvk ; Guddat et al., 1997[249] [Guddat, L. W., Bardwell, J. C. A., Zander, T. & Martin, J. L. (1997). Protein Sci. 6, 1148-1156.]-[250][bluearr.gif] ), coloured light green with the disulfide bond in yellow, is shown superimposed on the p73 [251][alpha] structure for comparison.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 545-551) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20150898 S.M.Di Pietro, D.Cascio, D.Feliciano, J.U.Bowie, and G.S.Payne (2010).
Regulation of clathrin adaptor function in endocytosis: novel role for the SAM domain.
  EMBO J, 29, 1033-1044.
PDB code: 3idw
20064379 H.H.Low, C.Sachse, L.A.Amos, and J.Löwe (2009).
Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving.
  Cell, 139, 1342-1352.
PDB code: 2w6d
19624732 S.Sollner, and P.Macheroux (2009).
New roles of flavoproteins in molecular cell biology: an unexpected role for quinone reductases as regulators of proteasomal degradation.
  FEBS J, 276, 4313-4324.  
18611950 W.H.Toh, E.Logette, L.Corcos, and K.Sabapathy (2008).
TAp73beta and DNp73beta activate the expression of the pro-survival caspase-2S.
  Nucleic Acids Res, 36, 4498-4509.  
14573615 S.J.Grimshaw, H.R.Mott, K.M.Stott, P.R.Nielsen, K.A.Evetts, L.J.Hopkins, D.Nietlispach, and D.Owen (2004).
Structure of the sterile alpha motif (SAM) domain of the Saccharomyces cerevisiae mitogen-activated protein kinase pathway-modulating protein STE50 and analysis of its interaction with the STE11 SAM.
  J Biol Chem, 279, 2192-2201.
PDB code: 1uqv
12624109 A.Cabral, D.F.Fischer, W.P.Vermeij, and C.Backendorf (2003).
Distinct functional interactions of human Skn-1 isoforms with Ese-1 during keratinocyte terminal differentiation.
  J Biol Chem, 278, 17792-17799.  
12954612 F.N.Barrera, J.A.Poveda, J.M.González-Ros, and J.L.Neira (2003).
Binding of the C-terminal sterile alpha motif (SAM) domain of human p73 to lipid membranes.
  J Biol Chem, 278, 46878-46885.  
12901798 Huqun, Y.Endo, H.Xin, M.Takahashi, T.Nukiwa, and K.Hagiwara (2003).
A naturally occurring p73 mutation in a p73-p53 double-mutant lung cancer cell line encodes p73 alpha protein with a dominant-negative function.
  Cancer Sci, 94, 718-724.  
14641909 M.Kollmar, and G.Glöckner (2003).
Identification and phylogenetic analysis of Dictyostelium discoideum kinesin proteins.
  BMC Genomics, 4, 47.  
12858164 T.Aviv, Z.Lin, S.Lau, L.M.Rendl, F.Sicheri, and C.A.Smibert (2003).
The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators.
  Nat Struct Biol, 10, 614-621.  
11992127 C.A.Kim, M.Gingery, R.M.Pilpa, and J.U.Bowie (2002).
The SAM domain of polyhomeotic forms a helical polymer.
  Nat Struct Biol, 9, 453-457.
PDB code: 1kw4
11809841 H.Nagaya, I.Wada, Y.J.Jia, and H.Kanoh (2002).
Diacylglycerol kinase delta suppresses ER-to-Golgi traffic via its SAM and PH domains.
  Mol Biol Cell, 13, 302-316.  
11825686 U.M.Moll, S.Erster, and A.Zaika (2001).
p53, p63 and p73--solos, alliances and feuds among family members.
  Biochim Biophys Acta, 1552, 47-59.  
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 code is shown on the right.