4D6D: Crystal Structure Of A Family 98 Glycoside Hydrolase Catalytic Module (sp3gh98) In Complex With The Blood Group A-trisaccharide (x02 Mutant)

Citation:
Abstract
Blood transfusions are critically important in many medical procedures, but the presence of antigens on red blood cells (RBCs, erythrocytes) means that careful blood-typing must be carried out prior to transfusion to avoid adverse and sometimes fatal reactions following transfusion. Enzymatic removal of the terminal N-acetylgalactosamine or galactose of A- or B-antigens, respectively, yields universal O-type blood, but is inefficient. Starting with the family 98 glycoside hydrolase from Streptococcus pneumoniae SP3-BS71 (Sp3GH98), which cleaves the entire terminal trisaccharide antigenic determinants of both A- and B-antigens from some of the linkages on RBC surface glycans, through several rounds of evolution, we developed variants with vastly improved activity toward some of the linkages that are resistant to cleavage by the wild-type enzyme. The resulting enzyme effects more complete removal of blood group antigens from cell surfaces, demonstrating the potential for engineering enzymes to generate antigen-null blood from donors of various types.
PDB ID: 4D6DDownload
MMDB ID: 124998
PDB Deposition Date: 2014/11/11
Updated in MMDB: 2014/11
Experimental Method:
x-ray diffraction
Resolution: 1.52  Å
Source Organism:
Similar Structures:
Biological Unit for 4D6D: monomeric; determined by author and by software (PISA)
Molecular Components in 4D6D
Label Count Molecule
Protein (1 molecule)
1
Glycoside Hydrolase
Molecule annotation
Chemicals (7 molecules)
1
1
2
1
3
1
4
1
5
3
* Click molecule labels to explore molecular sequence information.

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