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From Proteopedia
HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM
Structural highlights
FunctionTGM2_HUMAN Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTissue transglutaminase (TG) is a Ca2+-dependent acyltransferase with roles in cellular differentiation, apoptosis, and other biological functions. In addition to being a transamidase, TG undergoes a GTP-binding/GTPase cycle even though it lacks any obvious sequence similarity with canonical GTP-binding (G) proteins. Guanine nucleotide binding and Ca2+ concentration reciprocally regulate TG's transamidation activity, with nucleotide binding being the negative regulator. Here we report the x-ray structure determined to 2.8-A resolution of human TG complexed with GDP. Although the transamidation active site is similar to those of other known transglutaminases, the guanine nucleotide-binding site of TG differs markedly from other G proteins. The structure suggests a structural basis for the negative regulation of transamidation activity by bound nucleotide, and the positive regulation of transamidation by Ca2+. Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity.,Liu S, Cerione RA, Clardy J Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2743-7. Epub 2002 Feb 26. PMID:11867708[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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