-
Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.
Department of Biochemistry, University of Washington, Seattle 98195.
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'.
PMID: 7913750 [PubMed - indexed for MEDLINE]
PMCID: PMC44386
-
Cited by 19 PubMed Central articles
-
Transglutaminase 2 undergoes a large conformational change upon activation.
Pinkas DM, Strop P, Brunger AT, Khosla C.
PLoS Biol. 2007 Dec; 5(12):e327.
[PLoS Biol. 2007]
-
Transcriptome analysis of Pseudomonas putida in response to nitrogen availability.
Hervás AB, Canosa I, Santero E.
J Bacteriol. 2008 Jan; 190(1):416-20. Epub 2007 Oct 26.
[J Bacteriol. 2008]
-
Mechanism of allosteric regulation of transglutaminase 2 by GTP.
Begg GE, Carrington L, Stokes PH, Matthews JM, Wouters MA, Husain A, Lorand L, Iismaa SE, Graham RM.
Proc Natl Acad Sci U S A. 2006 Dec 26; 103(52):19683-8. Epub 2006 Dec 18.
[Proc Natl Acad Sci U S A. 2006]
- » See all...
Structures reported by this article