title: The application of NMR techniques to bacterial adhesins.
abstract: Extracellular adhesins frequently compose large, highly-ordered structural assemblies that project away from the bacterial surface. These assemblies, known as pili or fimbriae, are rod-like polymeric structures that in some cases can extend up to several micrometers from the cell surface. Because these adhesin structures are critical to bacterial colonization of host cell surfaces, there is an incentive to understand their structure, assembly and mechanism of host cell attachment. Various methods in Nuclear Magnetic Resonance (NMR) spectroscopy have been used to address these topics, yielding structural information at the atomic level. Also, new methods in solid-state NMR spectroscopy have thus far been under-utilized in the study of large adhesin structures and offer a powerful approach to overcoming problems with crystallization to better understand the structures of these complexes. The following is a brief overview of the contributions of NMR to the study of bacterial adhesins with an emphasis on the future potential of solid-state NMR.
authors.affiliation: Department of Pharmacology, Uniformed Services University of the Health Sciences, Bethesda, MD, 20814, USA. frank.shewmaker@usuhs.mil
authors.forename: Frank
authors.initials: F
authors.lastname: Shewmaker
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry*; D018830:Adhesins, Escherichia coli / Q000737:chemistry; D058227:Amyloidogenic Proteins / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D010861:Fimbriae, Bacterial / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*
chemical_list: D018829:Adhesins, Bacterial; D018830:Adhesins, Escherichia coli; D058227:Amyloidogenic Proteins; D001426:Bacterial Proteins; D005656:Fungal Proteins; C083891:HET-S protein, Podospora anserina; C077481:Crl protein, Bacteria