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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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| Hlavní autoři: | , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Public Library of Science (PLoS)
2012-01-01
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| Edice: | PLoS ONE |
| On-line přístup: | http://europepmc.org/articles/PMC3460858?pdf=render |
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