AI Article Synopsis
- Three high-resolution structures of the histidine triad protein from Entamoeba histolytica were determined at the Seattle Structural Genomics Center for Infectious Disease, which is linked to amoebic dysentery.
- * The structures show different molecules bound in the active site: sulfate, AMP, and GMP, with sulfate positioned similarly to the α-phosphate of the nucleotides.
- * The carbon alpha (C(α)) backbones of all three structures are nearly identical, with very small differences in their alignment (r.m.s.d.s between 0.06 and 0.13 Å).
Article Abstract
Three structures of the histidine triad family protein from Entamoeba histolytica, the causative agent of amoebic dysentery, were solved at high resolution within the Seattle Structural Genomics Center for Infectious Disease (SSGCID). The structures have sulfate (PDB entry 3oj7), AMP (PDB entry 3omf) or GMP (PDB entry 3oxk) bound in the active site, with sulfate occupying the same space as the α-phosphate of the two nucleotides. The C(α) backbones of the three structures are nearly superimposable, with pairwise r.m.s.d.s ranging from 0.06 to 0.13 Å.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4427167 | PMC |
| http://dx.doi.org/10.1107/S2053230X1500237X | DOI Listing |
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