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1kv3
From Proteopedia
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HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM
Overview
Tissue 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+.
About this Structure
1KV3 is a Single protein structure of sequence from Homo sapiens with GDP as ligand. Active as Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 17:55:05 2007
