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PDBsum entry 1a0b

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Histidine kinase PDB id
1a0b
Contents
Protein chain
117 a.a.
Metals
_ZN
Waters ×121

References listed in PDB file
Key reference
Title Insights into multistep phosphorelay from the crystal structure of the c-Terminal hpt domain of arcb.
Authors M.Kato, T.Mizuno, T.Shimizu, T.Hakoshima.
Ref. Cell, 1997, 88, 717-723. [DOI no: 10.1016/S0092-8674(00)81914-5]
PubMed id 9054511
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.
Figure 4.
Figure 4. Helix Structure and Sequence Alignment of HPt DomainsSide-view of helix D of the HPt domain of ArcB using a ball-and-stick model with the 2F[o]-F[c] electron density map. The imidazole ring makes a hydrogen bond to a water molecule (W).
Figure 5.
Figure 5. Comparison of HPt and P1 DomainsStructural comparison of the HPt domain of ArcB (right) and the P1 domain of CheA (left). The main chain is drawn as a ribbon in red for helices D and E of the HPt domain of ArcB and the corresponding part of CheA. The side chain of active His-717 of the HPt domain and the location of the corresponding histidine in the P1 domain are shown in green.
The above figures are reprinted by permission from Cell Press: Cell (1997, 88, 717-723) copyright 1997.
Secondary reference #1
Title Crystallization and preliminary X-Ray analysis of a histidine kinase domain of the anaerobic sensor protein arcb from escherichia coli.
Authors M.Kato, K.Ishige, T.Mizuno, T.Shimizu, T.Hakoshima.
Ref. Acta Crystallogr D Biol Crystallogr, 1996, 52, 1214-1215. [DOI no: 10.1107/S090744499600902X]
PubMed id 15299590
Full text Abstract
Figure 1.
Fig. 1. Crystal of ArcB c. The scale bar is 0.5 mm long.
The above figure is reproduced from the cited reference with permission from the IUCr
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