Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.

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'.

authors

Yee VC,Pedersen LC,Le Trong I,Bishop PD,Stenkamp RE,Teller DC

doi

10.1073/pnas.91.15.7296

subject

Has Abstract

pub_date

1994-07-19 00:00:00

pages

7296-300

issue

15

eissn

0027-8424

issn

1091-6490

journal_volume

91

pub_type

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