Báo cáo khoa học: The crystal structure of NlpI A prokaryotic tetratricopeptide repeat protein with a globular fold

The crystal structure of Nlpl

Tác giả: Christopher G. M. Wilson, Tommi Kajander, and Lynne Regan

Lĩnh vực: Molecular Biophysics and Biochemistry, Chemistry

Nội dung tài liệu: This study presents the high-resolution crystal structure of NlpI, a prokaryotic tetratricopeptide repeat (TPR) protein. Unlike many previously studied TPR proteins that fold into independent domains, the TPR motifs in NlpI are fully integrated into a globular protein structure. This research marks the first determination of a complete TPR-containing protein structure from a prokaryote. The findings indicate that NlpI’s structure is crucial for its role as a membrane-associated protein, influencing bacterial septation and virulence. The investigation also explores the potential for a ligand-binding cleft within the protein, suggesting a role in multiprotein assemblies.

Mục lục chi tiết:

• Abstract
• Keywords
• Correspondence
• (Received 7 September 2004, revised 19 September 2004, accepted 19 September 2004)
• doi:10.1111/j.1432-1033.2004.04397.x
• Introduction
• Results and Discussion
• Cloning and expression of Nipl
• Structure of mature Nipl
• Helix packing interactions
• TPRs
• NonTPR helix motifs
• Long-range interactions & globularity
• Quaternary organization
• Implications for function: a putative binding cleft
• Structural homologs
• Conclusion
• Experimental procedures
• Cloning Nipl constructs
• Expression and purification
• Size exclusion chromatography
• Crystallization of mature Nipl
• Data collection & phasing
• Model refinement
• Sequence and structure analysis
• Model coordinates
• Acknowledgements
• References