1g8m
From Proteopedia
Jump to navigationJump to search
CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION
| ||||||||||||
Structural highlights
FunctionPUR9_CHICK Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.[1] 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 PubMedATIC, the product of the purH gene, is a 64 kDa bifunctional enzyme that possesses the final two activities in de novo purine biosynthesis, AICAR transformylase and IMP cyclohydrolase. The crystal structure of avian ATIC has been determined to 1.75 A resolution by the MAD method using a Se-methionine modified enzyme. ATIC forms an intertwined dimer with an extensive interface of approximately 5,000 A(2) per monomer. Each monomer is composed of two novel, separate functional domains. The N-terminal domain (up to residue 199) is responsible for the IMPCH activity, whereas the AICAR Tfase activity resides in the C-terminal domain (200-593). The active sites of the IMPCH and AICAR Tfase domains are approximately 50 A apart, with no structural evidence of a tunnel connecting the two active sites. The crystal structure of ATIC provides a framework to probe both catalytic mechanisms and to design specific inhibitors for use in cancer chemotherapy and inflammation. Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis.,Greasley SE, Horton P, Ramcharan J, Beardsley GP, Benkovic SJ, Wilson IA Nat Struct Biol. 2001 May;8(5):402-6. PMID:11323713[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 04:32, 17 October 2024.