3LY6

Crystal structure of human transglutaminase 2 complex with adenosine 5' Triphosphate

Summary for 3LY6

• Entry DOI: 10.2210/pdb3ly6/pdb
• Descriptor: Protein-glutamine gamma-glutamyltransferase 2, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• Functional Keywords: transglutaminase, acyltransferase, diabetes mellitus, disease mutation, metal-binding, phosphoprotein, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 237675.73

Authors

Han, B.G.,Lee, B.I. (deposition date: 2010-02-26, release date: 2010-08-18, Last modification date: 2024-11-20)

Primary citation

Han, B.G.,Cho, J.W.,Cho, Y.D.,Jeong, K.C.,Kim, S.Y.,Lee, B.I.
Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate
Int.J.Biol.Macromol., 47:190-195, 2010

PubMed Abstract: Transglutaminase 2 (TG2) is a calcium-dependent multifunctional protein associated with various human diseases. We determined the crystal structure of human TG2 in complex with adenosine triphosphate (ATP). The ATP molecule binds to the previously identified guanosine diphosphate (GDP) binding pocket but has different hydrogen bonds and ion interaction with protein. The four residues Arg476, Arg478, Val479 and Tyr583, all of which are involved in both ATP and GDP binding by hydrogen bonds, might play important roles in the stabilization of TG2 by ATP or GDP. However, Ser482 and Arg580, which are involved in GDP binding, do not form hydrogen bond with ATP. Additionally, we newly discovered an intramolecular disulfide bond between Cys230 and Cys370, which formation might regulate the enzymatic activity of TG2.

PubMed: 20450932
DOI: 10.1016/j.ijbiomac.2010.04.023

Experimental method

X-RAY DIFFRACTION (3.14 Å)