6N1A

Crystal structure of an N-acetylgalactosamine deacetylase from F. plautii

Summary for 6N1A

• Entry DOI: 10.2210/pdb6n1a/pdb
• Descriptor: Carbohydrate-binding protein, MANGANESE (II) ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: n-acetylgalactosamine deacetylase, a blood antigen, cazy, hydrolase
• Biological source: Flavonifractor plautii
• Total number of polymer chains: 1
• Total formula weight: 56248.20

Authors

Sim, L.,Rahfeld, P.,Withers, S.G. (deposition date: 2018-11-08, release date: 2019-06-12, Last modification date: 2024-10-16)

Primary citation

Rahfeld, P.,Sim, L.,Moon, H.,Constantinescu, I.,Morgan-Lang, C.,Hallam, S.J.,Kizhakkedathu, J.N.,Withers, S.G.
An enzymatic pathway in the human gut microbiome that converts A to universal O type blood.
Nat Microbiol, 4:1475-1485, 2019

PubMed Abstract: Access to efficient enzymes that can convert A and B type red blood cells to 'universal' donor O would greatly increase the supply of blood for transfusions. Here we report the functional metagenomic screening of the human gut microbiome for enzymes that can remove the cognate A and B type sugar antigens. Among the genes encoded in our library of 19,500 expressed fosmids bearing gut bacterial DNA, we identify an enzyme pair from the obligate anaerobe Flavonifractor plautii that work in concert to efficiently convert the A antigen to the H antigen of O type blood, via a galactosamine intermediate. The X-ray structure of the N-acetylgalactosamine deacetylase reveals the active site and mechanism of the founding member of an esterase family. The galactosaminidase expands activities within the CAZy family GH36. Their ability to completely convert A to O of the same rhesus type at very low enzyme concentrations in whole blood will simplify their incorporation into blood transfusion practice, broadening blood supply.

PubMed: 31182795
DOI: 10.1038/s41564-019-0469-7

Experimental method

X-RAY DIFFRACTION (1.6 Å)