Protein folding modulates the swapped dimerization mechanism of methyl-accepting chemotaxis heme sensors.

The periplasmic sensor domains GSU0582 and GSU0935 are part of methyl accepting chemotaxis proteins in the bacterium Geobacter sulfurreducens. Both contain one c-type heme group and their crystal structures revealed that these domains form swapped dimers with a PAS fold formed from the two protein c...

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Bibliographic Details
Main Authors: Marta A Silva, Tânia G Lucas, Carlos A Salgueiro, Cláudio M Gomes
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2012-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3460858?pdf=render