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PDBsum entry 3ch5

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protein ligands metals Protein-protein interface(s) links
Transport protein PDB id
3ch5

 

 

 

 

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Contents
Protein chains
193 a.a. *
37 a.a. *
Ligands
SO4
GDP
Metals
_ZN
_MG
Waters ×71
* Residue conservation analysis
PDB id:
3ch5
Name: Transport protein
Title: The crystal structure of the rangdp-nup153znf2 complex
Structure: Gtp-binding nuclear protein ran. Chain: a. Synonym: gtpase ran. Ras-like protein tc4. Androgen receptor- associated protein 24. Engineered: yes. Fragment of nuclear pore complex protein nup153. Chain: b. Fragment: residues 703-754. Synonym: nup153znf2. Nucleoporin nup153.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ran, ara24. Expressed in: escherichia coli. Expression_system_taxid: 562. Rattus norvegicus. Rat. Organism_taxid: 10116.
Resolution:
2.10Å     R-factor:   0.198     R-free:   0.234
Authors: I.R.Vetter,N.Schrader
Key ref: N.Schrader et al. (2008). The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking site at the nuclear pore complex. Structure, 16, 1116-1125. PubMed id: 18611384
Date:
07-Mar-08     Release date:   01-Jul-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P62826  (RAN_HUMAN) -  GTP-binding nuclear protein Ran from Homo sapiens
Seq:
Struc:
216 a.a.
193 a.a.
Protein chain
Pfam   ArchSchema ?
P49791  (NU153_RAT) -  Nuclear pore complex protein Nup153 from Rattus norvegicus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1468 a.a.
37 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: Chain A: E.C.3.6.5.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 2: Chain B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

 
Structure 16:1116-1125 (2008)
PubMed id: 18611384  
 
 
The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking site at the nuclear pore complex.
N.Schrader, C.Koerner, K.Koessmeier, J.A.Bangert, A.Wittinghofer, R.Stoll, I.R.Vetter.
 
  ABSTRACT  
 
Nucleoporin (Nup) 153 is a highly mobile, multifunctional, and essential nuclear pore protein. It contains four zinc finger motifs that are thought to be crucial for the regulation of transport-receptor/cargo interactions via their binding to the small guanine nucleotide binding protein, Ran. We found this interaction to be independent of the phoshorylation state of the nucleotide. Ran binds with the highest affinity to the second zinc finger motif of Nup153 (Nup153ZnF2). Here we present the crystal structure of this complex, revealing a new type of Ran-Ran interaction partner interface together with the solution structure of Nup153ZnF2. According to our complex structure, Nup153ZnF2 binding to Ran excludes the formation of a Ran-importin-beta complex. This finding suggests a local Nup153-mediated Ran reservoir at the nucleoplasmic distal ring of the nuclear pore, where nucleotide exchange may take place in a ternary Nup153-Ran-RCC1 complex, so that import complexes are efficiently terminated.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19525551 J.A.DeGrasse, K.N.DuBois, D.Devos, T.N.Siegel, A.Sali, M.C.Field, M.P.Rout, and B.T.Chait (2009).
Evidence for a shared nuclear pore complex architecture that is conserved from the last common eukaryotic ancestor.
  Mol Cell Proteomics, 8, 2119-2130.  
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
19748337 S.G.Brohawn, J.R.Partridge, J.R.Whittle, and T.U.Schwartz (2009).
The nuclear pore complex has entered the atomic age.
  Structure, 17, 1156-1168.  
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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