4PYG

Transglutaminase2 complexed with GTP

Summary for 4PYG

• Entry DOI: 10.2210/pdb4pyg/pdb
• Descriptor: Protein-glutamine gamma-glutamyltransferase 2, GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: protein-gtp complex, transglutaminase fold, crosslinking, gtp binding, no modification, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 237021.10

Authors

Park, H.H.,Jang, T.H. (deposition date: 2014-03-27, release date: 2015-02-11, Last modification date: 2024-10-30)

Primary citation

Jang, T.H.,Lee, D.S.,Choi, K.,Jeong, E.M.,Kim, I.G.,Kim, Y.W.,Chun, J.N.,Jeon, J.H.,Park, H.H.
Crystal structure of transglutaminase 2 with GTP complex and amino acid sequence evidence of evolution of GTP binding site.
Plos One, 9:e107005-e107005, 2014

PubMed Abstract: Transglutaminase2 (TG2) is a multi-functional protein involved in various cellular processes, including apoptosis, differentiation, wound healing, and angiogenesis. The malfunction of TG2 causes many human disease including inflammatory disease, celiac disease, neurodegenerative diseases, tissue fibrosis, and cancers. Protein cross-linking activity, which is representative of TG2, is activated by calcium ions and suppressed by GTP. Here, we elucidated the structure of TG2 in complex with its endogenous inhibitor, GTP. Our structure showed why GTP is the optimal nucleotide for interacting with and inhibiting TG2. In addition, sequence comparison provided information describing the evolutionary scenario of GTP usage for controlling the activity of TG2.

PubMed: 25192068
DOI: 10.1371/journal.pone.0107005

Experimental method

X-RAY DIFFRACTION (2.8 Å)