The application of NMR techniques to bacterial adhesins.
Adv Exp Med Biol. 2011;715:241-56
Authors: Shewmaker F
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.
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Arch Biochem Biophys. 2004 Jan 15;421(2):186-91
Authors: Zhang J, Osborne JP, Gennis RB, Wang X
The heme environment and ligand binding properties of two relatively large membrane proteins containing multiple paramagnetic metal centers, cytochrome bo3 and bd quinol oxidases, have been studied by high field proton nuclear magnetic resonance (NMR) spectroscopy. The oxidized bo3 enzyme...
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[NMR paper] NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly
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J Mol Biol. 2002 Oct 11;323(1):143-51
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[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
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Biochemistry. 1997 Feb 18;36(7):1699-703
Authors: Wang J, Balazs YS, Thompson LK
The Escherichia coli serine receptor senses serine levels in the environment and transmits this information across the bacterial inner membrane to...
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[NMR paper] Bacterial overexpression, isotope enrichment, and NMR analysis of the N-terminal doma
Bacterial overexpression, isotope enrichment, and NMR analysis of the N-terminal domain of human apolipoprotein E.
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Biochem Cell Biol. 1997;75(1):45-53
Authors: Fisher CA, Wang J, Francis GA, Sykes BD, Kay CM, Ryan RO
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[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
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Biochemistry. 1997 Feb 18;36(7):1699-703
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[NMR paper] Bacterial overexpression, isotope enrichment, and NMR analysis of the N-terminal doma
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Biochem Cell Biol. 1997;75(1):45-53
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[NMR paper] Structural characterization of the divalent cation sites of bacterial phosphotriester
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Biochemistry. 1993 Sep 7;32(35):9148-55
Authors: Omburo GA, Mullins LS, Raushel FM
The phosphotriesterase from Pseudomonas diminuta catalyzes the hydrolysis of organophosphate esters. The isolated native protein contains zinc, and removal of this metal abolishes the enzymatic activity....
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[NMR paper] Bacterial expression and characterization of the CREB bZip module: circular dichroism
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Protein Sci. 1993 Sep;2(9):1461-71
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