1KV3

HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM

Summary for 1KV3

• Entry DOI: 10.2210/pdb1kv3/pdb
• Descriptor: Protein-glutamine gamma-glutamyltransferase, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: tissue transglutaminase; gtp binding protein; crystallography, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 6
• Total formula weight: 466708.82

Authors

Liu, S.,Cerione, R.A.,Clardy, J. (deposition date: 2002-01-24, release date: 2002-03-13, Last modification date: 2023-08-16)

Primary citation

Liu, S.,Cerione, R.A.,Clardy, J.
Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity.
Proc.Natl.Acad.Sci.USA, 99:2743-2747, 2002

PubMed Abstract: 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+.

PubMed: 11867708
DOI: 10.1073/pnas.042454899

Experimental method

X-RAY DIFFRACTION (2.8 Å)