| Literature DB >> 25945711 |
Donald D Lorimer1, Ryan Choi1, Ariel Abramov1, Stephen Nakazawa Hewitt1, Anna S Gardberg1, Wesley C Van Voorhis1, Bart L Staker1, Peter J Myler1, Thomas E Edwards1.
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.Entities:
Keywords: SSGCID; Seattle Structural Genomics Center for Infectious Disease; hydrolase; metal-binding protein; structural genomics
Mesh：
Substances：
Year: 2015 PMID： 25945711 PMCID： PMC4427167 DOI： 10.1107/S2053230X1500237X
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN： 2053-230X Impact factor: 1.056