6t8s
From Proteopedia
Structure of the major Type IV pilin PilA1 from Clostridium difficile
Structural highlights
Publication Abstract from PubMedMany biologists are now routinely seeking to determine the three-dimensional structures of their proteins of choice, illustrating the importance of this knowledge, but also of the simplification and streamlining of structure-determination processes. Despite the fact that most software packages offer simple pipelines, for the non-expert navigating the outputs and understanding the key aspects can be daunting. Here, the structure determination of the type IV pili (TFP) protein PilA1 from Clostridioides difficile is used to illustrate the different steps involved, the key decision criteria and important considerations when using the most common pipelines and software. Molecular-replacement pipelines within CCP4i2 are presented to illustrate the more commonly used processes. Previous knowledge of the biology and structure of TFP pilins, particularly the presence of a long, N-terminal alpha-helix required for pilus formation, allowed informed decisions to be made during the structure-determination strategy. The PilA1 structure was finally successfully determined using ARCIMBOLDO and the ab initio MR strategy used is described. A practical overview of molecular replacement: Clostridioides difficile PilA1, a difficult case study.,Crawshaw AD, Basle A, Salgado PS Acta Crystallogr D Struct Biol. 2020 Mar 1;76(Pt 3):261-271. doi:, 10.1107/S2059798320000467. Epub 2020 Feb 26. PMID:32133990[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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