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PDBsum entry 2c6b

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protein metals links
Ligase PDB id
2c6b

 

 

 

 

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Contents
Protein chain
46 a.a. *
Metals
_ZN
* Residue conservation analysis
PDB id:
2c6b
Name: Ligase
Title: Solution structure of the c4 zinc-finger domain of hdm2
Structure: Ubiquitin-protein ligase e3 mdm2. Chain: a. Synonym: human mdm2, p53-binding protein mdm2, oncoprotein mdm2, double minute 2 protein, hdm2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: c41.
NMR struc: 20 models
Authors: G.W.Yu,M.D.Allen,A.Andreeva,A.R.Fersht,M.Bycroft
Key ref:
G.W.Yu et al. (2006). Solution structure of the C4 zinc finger domain of HDM2. Protein Sci, 15, 384-389. PubMed id: 16385008 DOI: 10.1110/ps.051927306
Date:
08-Nov-05     Release date:   04-Jan-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q00987  (MDM2_HUMAN) -  E3 ubiquitin-protein ligase Mdm2 from Homo sapiens
Seq:
Struc:
491 a.a.
46 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.2.27  - RING-type E3 ubiquitin transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine

 

 
DOI no: 10.1110/ps.051927306 Protein Sci 15:384-389 (2006)
PubMed id: 16385008  
 
 
Solution structure of the C4 zinc finger domain of HDM2.
G.W.Yu, M.D.Allen, A.Andreeva, A.R.Fersht, M.Bycroft.
 
  ABSTRACT  
 
HDM2 is a ubiquitin E3 ligase that is a key negative regulator of the tumor suppressor p53. Here, we report the determination of the solution structure of the C4 zinc finger domain of HDM2 using multidimensional NMR. The HDM2 C4 zinc finger domain has a fold consisting of a 3(10) helix followed by four beta-strands, which shares significant structural similarity to the zinc ribbon protein family. Family based sequence analysis identified two putative binding sites, one of which resembles an RNA binding motif.
 
  Selected figure(s)  
 
Figure 1.
NMR structures of the cis and trans forms of the HDM2 C4 zinc finger domain. An overlay of the backbone atoms of the 20 lowest energy NMR structures for the (A) trans and (B) cis forms of the HDM2 C4 zinc finger. (C) A ribbon representation of the trans (blue) and cis (red) conformers superimposed over the folded region, prepared using the program MOLSCRIPT (Kraulis 1991).
Figure 3.
Comparison of zinc knuckles of HDM2 and Isoleucyl-tRNA synthetase. (A) MDM2; (B) Isoleucyl-tRNA synthetase (1ffy:A) boundto tRNA. Conserved Trp, Arg, and Cys are shown as sticks. The figure was produced using Pymol (DeLanoScientific).
 
  The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2006, 15, 384-389) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21134643 E.Escobar-Cabrera, D.K.Lau, S.Giovinazzi, A.M.Ishov, and L.P.McIntosh (2010).
Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C.
  Structure, 18, 1642-1653.
PDB codes: 2kzs 2kzu
20856878 L.Jelsbak, H.Ingmer, L.Valihrach, M.T.Cohn, M.H.Christiansen, B.H.Kallipolitis, and D.Frees (2010).
The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.
  PLoS One, 5, e12752.  
19568783 E.G.Worrall, B.Wawrzynow, L.Worrall, M.Walkinshaw, K.L.Ball, and T.R.Hupp (2009).
Regulation of the E3 ubiquitin ligase activity of MDM2 by an N-terminal pseudo-substrate motif.
  J Chem Biol, 2, 113-129.  
19304800 F.E.Loughlin, R.E.Mansfield, P.M.Vaz, A.P.McGrath, S.Setiyaputra, R.Gamsjaeger, E.S.Chen, B.J.Morris, J.M.Guss, and J.P.Mackay (2009).
The zinc fingers of the SR-like protein ZRANB2 are single-stranded RNA-binding domains that recognize 5' splice site-like sequences.
  Proc Natl Acad Sci U S A, 106, 5581-5586.
PDB code: 3g9y
19505478 J.R.Partridge, and T.U.Schwartz (2009).
Crystallographic and biochemical analysis of the Ran-binding zinc finger domain.
  J Mol Biol, 391, 375-389.
PDB codes: 3gj0 3gj3 3gj4 3gj5 3gj6 3gj7 3gj8
19878869 Y.Zhang, and H.Lu (2009).
Signaling to p53: ribosomal proteins find their way.
  Cancer Cell, 16, 369-377.  
18755053 A.J.Schoeffler, and J.M.Berger (2008).
DNA topoisomerases: harnessing and constraining energy to govern chromosome topology.
  Q Rev Biophys, 41, 41.  
18713742 E.Bitto, C.A.Bingman, L.Bittova, D.A.Kondrashov, R.M.Bannen, B.G.Fox, J.L.Markley, and G.N.Phillips (2008).
Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain.
  J Biol Chem, 283, 30184-30192.
PDB code: 3bvo
18611384 N.Schrader, C.Koerner, K.Koessmeier, J.A.Bangert, A.Wittinghofer, R.Stoll, and I.R.Vetter (2008).
The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking site at the nuclear pore complex.
  Structure, 16, 1116-1125.
PDB codes: 2k0c 3ch5
18809412 S.G.Sivakolundu, A.Nourse, S.Moshiach, B.Bothner, C.Ashley, J.Satumba, J.Lahti, and R.W.Kriwacki (2008).
Intrinsically unstructured domains of Arf and Hdm2 form bimolecular oligomeric structures in vitro and in vivo.
  J Mol Biol, 384, 240-254.  
17116689 M.S.Lindström, A.Jin, C.Deisenroth, G.White Wolf, and Y.Zhang (2007).
Cancer-associated mutations in the MDM2 zinc finger domain disrupt ribosomal protein interaction and attenuate MDM2-induced p53 degradation.
  Mol Cell Biol, 27, 1056-1068.  
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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