1GGT

THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII

Summary for 1GGT

• Entry DOI: 10.2210/pdb1ggt/pdb
• Descriptor: COAGULATION FACTOR XIII (1 entity in total)
• Functional Keywords: blood coagulation
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P00488
• Total number of polymer chains: 2
• Total formula weight: 166467.84

Authors

Yee, V.C.,Pedersen, L.C.,Trong, I.L.,Bishop, P.D.,Stenkamp, R.E.,Teller, D.C. (deposition date: 1994-01-25, release date: 1995-07-31, Last modification date: 2024-02-07)

Primary citation

Yee, V.C.,Pedersen, L.C.,Le Trong, I.,Bishop, P.D.,Stenkamp, R.E.,Teller, D.C.
Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.
Proc.Natl.Acad.Sci.USA, 91:7296-7300, 1994

PubMed Abstract: Mechanical stability in many biological materials is provided by the crosslinking of large structural proteins with gamma-glutamyl-epsilon-lysyl amide bonds. The three-dimensional structure of human recombinant factor XIII (EC 2.3.2.13 zymogen; protein-glutamine:amine gamma-glutamyltransferase a chain), a transglutaminase zymogen, has been solved at 2.8-A resolution by x-ray crystallography. This structure shows that each chain of the homodimeric protein is folded into four sequential domains. A catalytic triad reminiscent of that observed in cysteine proteases has been identified in the core domain. The amino-terminal activation peptide of each subunit crosses the dimer interface and partially occludes the opening of the catalytic cavity in the second subunit, preventing substrate binding to the zymogen. A proposal for the mechanism of activation by thrombin and calcium is made that details the structural events leading to active factor XIIIa'.

PubMed: 7913750
DOI: 10.1073/pnas.91.15.7296

Experimental method

X-RAY DIFFRACTION (2.65 Å)