4AC8

R2-like ligand binding Mn-Fe oxidase from M. tuberculosis with an organized C-terminal helix

Summary for 4AC8

• Entry DOI: 10.2210/pdb4ac8/pdb
• Descriptor: R2-LIKE LIGAND BINDING OXIDASE, FE (III) ION, MANGANESE (II) ION, ... (7 entities in total)
• Functional Keywords: oxidoreductase, dimetal cofactor, monooxygenase, metalloprotein
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 4
• Total formula weight: 148669.73

Authors

Andersson, C.S.,Berthold, C.L.,Hogbom, M. (deposition date: 2011-12-14, release date: 2012-09-26, Last modification date: 2023-12-20)

Primary citation

Andersson, C.S.,Berthold, C.L.,Hogbom, M.
A Dynamic C-Terminal Segment in the Mycobacterium Tuberculosis Mn/Fe R2Lox Protein Can Adopt a Helical Structure with Possible Functional Consequences.
Chem.Biodivers., 9:1981-, 2012

PubMed Abstract: Mycobacterium tuberculosis R2-like ligand-binding oxidase (MtR2lox) belongs to a recently discovered group of proteins that are homologous to the ribonucleotide reductase R2 proteins. MtR2lox carries a heterodinuclear Mn/Fe cofactor and, unlike R2 proteins, a large ligand-binding cavity. A unique tyrosine-valine cross link is also found in the vicinity of the active site. To date, all known structures of R2 and R2lox proteins show a disordered C-terminal segment. Here, we present two new crystal forms of MtR2lox, revealing an ordered helical C-terminal. The ability of alternating between an ordered and disordered state agrees well with bioinformatic analysis of the protein sequence. Interestingly, ordering of the C-terminal helix shields a large positively charged patch on the protein surface, potentially used for interaction with other cellular components. We hypothesize that the dynamic C-terminal segment may be involved in control of protein function in vivo.

PubMed: 22976985
DOI: 10.1002/CBDV.201100428

Experimental method

X-RAY DIFFRACTION (2.75 Å)