2BDX: X-Ray Crystal Structure Of Dihydromicrocystin-La Bound To Protein Phosphatase-1

Citation:
Abstract
The microcystins and nodularins are tumour promoting hepatotoxins that are responsible for global adverse human health effects and wildlife fatalities in countries where drinking water supplies contain cyanobacteria. The toxins function by inhibiting broad specificity Ser/Thr protein phosphatases in the host cells, thereby disrupting signal transduction pathways. A previous crystal structure of a microcystin bound to the catalytic subunit of protein phosphatase-1 (PP-1c) showed distinct changes in the active site region when compared with protein phosphatase-1 structures bound to other toxins. We have elucidated the crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c (gamma isoform). The atomic structures of these complexes reveal the structural basis for inhibition of protein phosphatases by these toxins. Comparisons of the structures of the cyanobacterial toxin:phosphatase complexes explain the biochemical mechanism by which microcystins but not nodularins permanently modify their protein phosphatase targets by covalent addition to an active site cysteine residue.
PDB ID: 2BDXDownload
MMDB ID: 93085
PDB Deposition Date: 2005/10/21
Updated in MMDB: 2011/08
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 2BDX: dimeric; determined by author
Molecular Components in 2BDX
Label Count Molecule
Protein (1 molecule)
1
Serine/threonine Protein Phosphatase Pp1-gamma Catalytic Subunit(Gene symbol: PPP1CC)
Molecule annotation
Nucleotide(1 molecule)
1
Dihydromicrocystin-la
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.