2qkd
From Proteopedia
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|PDB= 2qkd |SIZE=350|CAPTION= <scene name='initialview01'>2qkd</scene>, resolution 2.00Å  | |PDB= 2qkd |SIZE=350|CAPTION= <scene name='initialview01'>2qkd</scene>, resolution 2.00Å  | ||
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+501'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+502'>AC2</scene> and <scene name='pdbsite=AC3:Fmt+Binding+Site+For+Residue+A+778'>AC3</scene>  | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+501'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+502'>AC2</scene> and <scene name='pdbsite=AC3:Fmt+Binding+Site+For+Residue+A+778'>AC3</scene>  | ||
| - | |LIGAND= <scene name='pdbligand=  | + | |LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>  | 
|ACTIVITY=   | |ACTIVITY=   | ||
|GENE= Znf259, Zfp259, Zpr1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])  | |GENE= Znf259, Zfp259, Zpr1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])  | ||
| + | |DOMAIN=  | ||
| + | |RELATEDENTRY=  | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qkd OCA], [http://www.ebi.ac.uk/pdbsum/2qkd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qkd RCSB]</span>  | ||
}}  | }}  | ||
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[[Category: Single protein]]  | [[Category: Single protein]]  | ||
[[Category: Mishra, A K.]]  | [[Category: Mishra, A K.]]  | ||
| - | [[Category: FMT]]  | ||
| - | [[Category: ZN]]  | ||
[[Category: anti-parrallel beta sheet]]  | [[Category: anti-parrallel beta sheet]]  | ||
[[Category: beta helix]]  | [[Category: beta helix]]  | ||
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[[Category: signaling protein]]  | [[Category: signaling protein]]  | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on   | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:50:15 2008''  | 
Revision as of 01:50, 31 March 2008
 
 
  | |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , | ||||||
| Gene: | Znf259, Zfp259, Zpr1 (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of tandem ZPR1 domains
Overview
Eukaryotic genomes encode a zinc finger protein (ZPR1) with tandem ZPR1 domains. In response to growth stimuli, ZPR1 assembles into complexes with eukaryotic translation elongation factor 1A (eEF1A) and the survival motor neurons protein. To gain insight into the structural mechanisms underlying the essential function of ZPR1 in diverse organisms, we determined the crystal structure of a ZPR1 domain tandem and characterized the interaction with eEF1A. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. However, ZPR1 efficiently displaces the exchange factor eEF1Balpha from preformed nucleotide-free complexes, suggesting that it may function as a negative regulator of eEF1A activation. Structure-based mutational and complementation analyses reveal a conserved binding epitope for eEF1A that is required for normal cell growth, proliferation, and cell cycle progression. Structural differences between the ZPR1 domains contribute to the observed functional divergence and provide evidence for distinct modalities of interaction with eEF1A and survival motor neuron complexes.
About this Structure
2QKD is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes., Mishra AK, Gangwani L, Davis RJ, Lambright DG, Proc Natl Acad Sci U S A. 2007 Aug 28;104(35):13930-5. Epub 2007 Aug 17. PMID:17704259
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