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PDBsum entry 1drm

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Transferase PDB id
1drm
Contents
Protein chain
119 a.a. *
Ligands
HEM
Waters ×82
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structure of a biological oxygen sensor: a new mechanism for heme-Driven signal transduction.
Authors W.Gong, B.Hao, S.S.Mansy, G.Gonzalez, M.A.Gilles-Gonzalez, M.K.Chan.
Ref. Proc Natl Acad Sci U S A, 1998, 95, 15177-15182. [DOI no: 10.1073/pnas.95.26.15177]
PubMed id 9860942
Abstract
The FixL proteins are biological oxygen sensors that restrict the expression of specific genes to hypoxic conditions. FixL's oxygen-detecting domain is a heme binding region that controls the activity of an attached histidine kinase. The FixL switch is regulated by binding of oxygen and other strong-field ligands. In the absence of bound ligand, the heme domain permits kinase activity. In the presence of bound ligand, this domain turns off kinase activity. Comparison of the structures of two forms of the Bradyrhizobium japonicum FixL heme domain, one in the "on" state without bound ligand and one in the "off" state with bound cyanide, reveals a mechanism of regulation by a heme that is distinct from the classical hemoglobin models. The close structural resemblance of the FixL heme domain to the photoactive yellow protein confirms the existence of a PAS structural motif but reveals the presence of an alternative regulatory gateway.
Figure 3.
Fig. 3. Ball-and-stick diagrams of three heme-binding pockets. Structures are shown for Glycera dibranchiata hemoglobin (PDB ID: 2HBG) (Left), BjFixLH (Center), and the NO transporter protein (PDB ID: 1NP1) (Right) (27, 28). The rightmost and leftmost side chains correspond to the E7 and E11 residues of hemoglobins, respectively. The additional side chain in BjFixLH (red) corresponds to Ile 215. The structures were aligned based on the orientation of the proximal histidine and the porphyrin ring. The atoms are colored as in Fig. 1.
Figure 5.
Fig. 5. Comparison of the structures of the regulatory FG loop of BjFixLH in the unliganded "on" and cyanide bound "off" states. (A) The structure of the FG loop in the met-BjFixLH (brown) illustrating the hydrogen-bonding interactions (Left) and 2F[O]-F[C] electron density map (1 ) (Right). (B) Corresponding figure for cyanomet-BjFixLH (blue) showing hydrogen bonding (Left) and electron density (Right). (C) Stereoview of overlap of the refined models for both states.
PROCHECK
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 Headers

 

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