Figure S2 from Structural Insight into Geranylgeranyl Diphosphate Synthase (GGDPS) for Cancer Therapy
Year: 2024
Type: other
Abstract: AlphaFold model of an hGGDPS monomer (hGGDPSAF) and sequence alignment of hGGDPS with yGGDPS. A. Regions are colored based on the per-residue confidence scores (pLDDT) ranging from 0 – 100 with higher scores reflecting well-defined parts of the structure. Residues which show a “very high” confidence score have been determined with supporting crystal structures. These residues include those at the active site. Disordered loops that have not been structurally established are shown to have “confident” scores (His194-Phe204, Leu22-Thr29). The N-terminal (Met1-Lys3) and C-terminal ends (Glu297-Glu300) are very disordered and are shown to have “low” and “very low” confidence scores. B. A sequence alignment of the conservation of residues between yGGDPS and hGGDPS. Conserved residues are colored in a dark blue while unconserved residues are colored a light blue. A pairwise alignment calculation found yGGDPS and hGGDPS to be 39.2% similar. Asterisks represent binding sites for the respective ligands as indicated in the legend. Allignment was performed with the Jalview software of Saccharomyces cerevisiae GGDPS (yGGDPS Uniprot: Q12051, top) and Homo sapiens GGDPS (hGGDPS Uniprot: O95749, bottom). C. Sequence alignment highlighting the conservation of residue properties. Helices are shown as red cylinders and are numbered sequentially. Residues contributing to IPP, FDP, and GGDP binding are shown as colored asterisks.
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
OpenAlex ID: W4390540196