NDLI: Diagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identity.

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Diagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identity.

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Diagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identity.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lai, Wing-Cheung Lybrand, Terry P. Hazelbauer, Gerald L. Peach, Megan L.
Description	Country affiliation: United States Author Affiliation: Lai WC ( Department of Biochemistry, University of Missouri-Columbia, Columbia, MO 65211, USA.)
Abstract	Hundreds of bacterial chemoreceptors from many species have periplasmic, ligand-recognition domains of approximately the same size, but little or no sequence identity. The only structure determined is for the periplasmic domain of chemoreceptor Tar from Salmonella and Escherichia coli. Do sequence-divergent but similarly sized chemoreceptor periplasmic domains have related structures? We addressed this issue for the periplasmic domain of chemoreceptor Trg(E) from E. coli, which has a low level of sequence similarity to Tar, by combining homology modeling and diagnostic cross-linking between pairs of introduced cysteines. A homology model of the Trg(E) domain was created using the homodimeric, four-helix bundle structure of the Tar(S) domain from Salmonella. In this model, we chose four pairs of positions at which introduced cysteines would be sufficiently close to form disulfides across each of four different helical interfaces. For each pair we chose a second pair, in which one cysteine of the original pair was shifted by one position around the helix and thus would be less favorably placed for disulfide formation. We created genes coding for proteins containing four such pairs of cysteine pairs and investigated disulfide formation in vivo as well as functional consequences of the substitutions and disulfides between neighboring helices. Results of the experimental tests provided strong support for the accuracy of the model, indicating that the Trg(E) periplasmic domain is very similar to the Tar(S) domain. Diagnostic cross-linking of paired pairs of introduced cysteines could be applied generally as a stringent test of homology models.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	1
Volume Number	15
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2006-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Chemoreceptor Cells Chemistry Cysteine Metabolism Escherichia Coli Proteins Membrane Proteins Receptors, Cell Surface Structural Homology, Protein Amino Acid Sequence Amino Acid Substitution Genetics Bacterial Proteins Chemotaxis Physiology Cross-linking Reagents Disulfides Escherichia Coli Models, Molecular Molecular Sequence Data Periplasm Protein Structure, Tertiary Research Support, N.i.h., Extramural Validation Studies Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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