6EU8
Crystal structure of Tannerella forsythia Apo HmuY analog (TFO)
Summary for 6EU8
| Entry DOI | 10.2210/pdb6eu8/pdb |
| Descriptor | Putative heme binding protein, MALONATE ION (3 entities in total) |
| Functional Keywords | heme-binding protein |
| Biological source | Tannerella forsythia (Bacteroides forsythus) |
| Total number of polymer chains | 1 |
| Total formula weight | 22517.92 |
| Authors | Antonyuk, S.V.,Strange, R.W. (deposition date: 2017-10-29, release date: 2018-10-24, Last modification date: 2024-01-17) |
| Primary citation | Bielecki, M.,Antonyuk, S.,Strange, R.W.,Smalley, J.W.,Mackiewicz, P.,Smiga, M.,Stepien, P.,Olczak, M.,Olczak, T. Tannerella forsythiaTfo belongs toPorphyromonas gingivalisHmuY-like family of proteins but differs in heme-binding properties. Biosci. Rep., 38:-, 2018 Cited by PubMed Abstract: is considered the principal etiologic agent and keystone pathogen of chronic periodontitis. As an auxotrophic bacterium, it must acquire heme to survive and multiply at the infection site. HmuY is the first member of a novel family of hemophore-like proteins. Bacterial heme-binding proteins usually use histidine-methionine or histidine-tyrosine residues to ligate heme-iron, whereas HmuY uses two histidine residues. We hypothesized that other 'red complex' members, i.e. and might utilize similar heme uptake mechanisms to the HmuY. Comparative and phylogenetic analyses suggested differentiation of HmuY homologs and low conservation of heme-coordinating histidine residues present in HmuY. The homologs were subjected to duplication before divergence of lineages, which could facilitate evolution of functional diversification. We found that does not code an HmuY homolog. protein, termed as Tfo, binds heme, but preferentially in the ferrous form, and sequesters heme from the albumin-heme complex under reducing conditions. In agreement with that, the 3D structure of Tfo differs from that of HmuY in the folding of heme-binding pocket, containing two methionine residues instead of two histidine residues coordinating heme in HmuY. Heme binding to apo-HmuY is accompanied by movement of the loop carrying the His residue, closing the heme-binding pocket. Molecular dynamics simulations (MD) demonstrated that this conformational change also occurs in Tfo. In conclusion, our findings suggest that HmuY-like family might comprise proteins subjected during evolution to significant diversification, resulting in different heme-binding properties. PubMed: 30266745DOI: 10.1042/BSR20181325 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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