4LYG: Crystal Structure Of Human Prs1 E43t Mutant

Citation:
Abstract
Human PRS1, which is indispensable for the biosynthesis of nucleotides, deoxynucleotides and their derivatives, is associated directly with multiple human diseases because of single base mutation. However, a molecular understanding of the effect of these mutations is hampered by the lack of understanding of its catalytic mechanism. Here, we reconstruct the 3D EM structure of the PRS1 apo state. Together with the native stain EM structures of AMPNPP, AMPNPP and R5P, ADP and the apo states with distinct conformations, we suggest the hexamer is the enzymatically active form. Based on crystal structures, sequence analysis, mutagenesis, enzyme kinetics assays, and MD simulations, we reveal the conserved substrates binding motifs and make further analysis of all pathogenic mutants.
PDB ID: 4LYGDownload
MMDB ID: 126613
PDB Deposition Date: 2013/7/31
Updated in MMDB: 2015/03
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 4LYG: hexameric; determined by author and by software (PISA)
Molecular Components in 4LYG
Label Count Molecule
Proteins (6 molecules)
6
Ribose-phosphate Pyrophosphokinase 1(Gene symbol: PRPS1)
Molecule annotation
Chemicals (15 molecules)
1
15
* Click molecule labels to explore molecular sequence information.

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