6DE6

2.1 A resolution structure of histamine dehydrogenase from Rhizobium sp. 4-9

Summary for 6DE6

• Entry DOI: 10.2210/pdb6de6/pdb
• Descriptor: Histamine dehydrogenase, ADENOSINE-5'-DIPHOSPHATE, FLAVIN MONONUCLEOTIDE, ... (6 entities in total)
• Functional Keywords: histamine dehydrogenase, fmn binding, 4fe-4s cluster, oxidoreductase
• Biological source: Rhizobium sp. 4-9
• Total number of polymer chains: 2
• Total formula weight: 156765.84

Authors

Goyal, P.,Lovell, S.,Richter, M. (deposition date: 2018-05-11, release date: 2019-05-15, Last modification date: 2024-10-23)

Primary citation

Goyal, P.,Deay 3rd, D.,Seibold, S.,Candido, A.C.L.,Lovell, S.,Battaile, K.P.,Wilson, G.S.,Richter, M.L.,Petillo, P.A.
Structure of Rhizobium sp. 4-9 histamine dehydrogenase and analysis of the electron transfer pathway to an abiological electron acceptor.
Arch.Biochem.Biophys., :109612-109612, 2023

PubMed Abstract: Histamine dehydrogenase from the gram-negative bacterium Rhizobium sp. 4-9 (HaDHR) is a member of a small family of dehydrogenases containing a covalently attached FMN, and the only member so far identified to date that does not exhibit substrate inhibition. In this study, we present the 2.1 Å resolution crystal structure of HaDHR. This new structure allowed for the identification of the internal electron transfer pathway to abiological ferrocene-based mediators. Alanine 437 was identified as the exit point of electrons from the FeS cluster. The enzyme was modified with a Ser436Cys mutation to facilitate covalent attachment of a ferrocene moiety. When modified with Fc-maleimide, this new construct demonstrated direct electron transfer from the enzyme to a gold electrode in a histamine concentration-dependent manner without the need for any additional electron mediators.

PubMed: 37146865
DOI: 10.1016/j.abb.2023.109612

Experimental method

X-RAY DIFFRACTION (2.1 Å)