9HMU
DUF4465 domain containing protein in complex with vitamin B12.
Summary for 9HMU
| Entry DOI | 10.2210/pdb9hmu/pdb |
| Related | 9FCT |
| Descriptor | DUF4465 domain containing protein D5EK, CYANOCOBALAMIN, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | complex, vitamin b12, bacteria, scavenging, outer membrane, membrane associated, membrane protein |
| Biological source | Coraliomargarita akajimensis |
| Total number of polymer chains | 3 |
| Total formula weight | 85028.00 |
| Authors | Clarke, C.,Banasik, M.,Pickersgill, R.W. (deposition date: 2024-12-09, release date: 2025-01-15, Last modification date: 2026-08-12) |
| Primary citation | Clarke, C.,Banasik, M.,Juodeikis, R.,Warren, M.J.,Pickersgill, R.W. Evolutionarily divergent DUF4465 domains have a common vitamin B 12 -binding function. Febs Open Bio, 16:1537-1549, 2026 Cited by PubMed Abstract: The DUF4465 family (DUF, domain of unknown function) contains more than 1000 members distributed across eight bacterial clades with species from diverse microenvironments including various gut microbiomes, hydrothermal vents, and soil. In the gut commensal Bacteroides thetaiotaomicron (B. theta), DUF4465 containing proteins act as high-affinity B-binding proteins that scavenge this cofactor to ensure bacterial survival. Such B capture is essential for bacteria that have lost the ability to synthesize B de novo. This raises the question of whether B-binding is ubiquitous across this family of proteins. Here, we show that B-binding is a recurrent function of eight distantly related members of the DUF4465 family. It is reasonable to conclude that B-binding is a common function of most DUF4465 proteins. These results establish DUF4465 as a structurally conserved family of augmented β-jellyroll B-binding proteins with widespread roles in microbial competition for this essential cofactor. Impact statement DUF4465 defines a widespread, structurally conserved bacterial cobalamin-binding domain and provides a promising scaffold for protein-based B capture and purification. PubMed: 41846281DOI: 10.1002/2211-5463.70231 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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