1a0b
From Proteopedia
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'''HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ARCB FROM ESCHERICHIA COLI''' | '''HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ARCB FROM ESCHERICHIA COLI''' | ||
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[[Category: Mizuno, T.]] | [[Category: Mizuno, T.]] | ||
[[Category: Shimizu, T.]] | [[Category: Shimizu, T.]] | ||
| - | [[Category: | + | [[Category: Four-helix bundle]] |
| - | [[Category: | + | [[Category: Histidine kinase]] |
| - | [[Category: | + | [[Category: Phosphotransfer]] |
| - | [[Category: | + | [[Category: Two-component system]] |
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Revision as of 06:37, 2 May 2008
HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ARCB FROM ESCHERICHIA COLI
Overview
The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined at 2.06 A resolution. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes.
About this Structure
1A0B is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB., Kato M, Mizuno T, Shimizu T, Hakoshima T, Cell. 1997 Mar 7;88(5):717-23. PMID:9054511 Page seeded by OCA on Fri May 2 09:37:10 2008
