Format

Send to

Choose Destination
Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):572-6. doi: 10.1107/S2053230X1500237X. Epub 2015 Apr 21.

Structures of a histidine triad family protein from Entamoeba histolytica bound to sulfate, AMP and GMP.

Author information

1
Seattle Structural Genomics Center for Infectious Disease, USA.

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.

KEYWORDS:

SSGCID; Seattle Structural Genomics Center for Infectious Disease; hydrolase; metal-binding protein; structural genomics

PMID:
25945711
PMCID:
PMC4427167
DOI:
10.1107/S2053230X1500237X
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for International Union of Crystallography Icon for PubMed Central
Loading ...
Support Center