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1A0B

HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ARCB FROM ESCHERICHIA COLI

Summary for 1A0B
Entry DOI10.2210/pdb1a0b/pdb
DescriptorAEROBIC RESPIRATION CONTROL SENSOR PROTEIN ARCB, ZINC ION (3 entities in total)
Functional Keywordshistidine kinase, phosphotransfer, two-component system, four-helix bundle
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight14079.35
Authors
Kato, M.,Mizuno, T.,Shimizu, T.,Hakoshima, T. (deposition date: 1997-11-27, release date: 1998-03-18, Last modification date: 2024-02-07)
Primary citationKato, M.,Mizuno, T.,Shimizu, T.,Hakoshima, T.
Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB.
Cell(Cambridge,Mass.), 88:717-723, 1997
Cited by
PubMed Abstract: 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.
PubMed: 9054511
DOI: 10.1016/S0092-8674(00)81914-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.06 Å)
Structure validation

237735

数据于2025-06-18公开中

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