ArticleActa crystallographica. Section F, Structural biology communications2015
Structures of a histidine triad family protein from Entamoeba histolytica bound to sulfate, AMP and GMP.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 3 citations in OpenAlex.
- Response to Errors in Crystal structure of HINT from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Crystal structure of HINT from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2016Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
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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