1g8m
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1g8m.jpg|left|200px]] | [[Image:1g8m.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1g8m", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1g8m| PDB=1g8m | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION''' | '''CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION''' | ||
| Line 32: | Line 29: | ||
[[Category: 1 alpha + beta domain]] | [[Category: 1 alpha + beta domain]] | ||
[[Category: 2 functional domain]] | [[Category: 2 functional domain]] | ||
| - | [[Category: | + | [[Category: Aicar tfase = 2 alpha/beta/alpha domain]] |
| - | [[Category: | + | [[Category: Homodimer]] |
| - | [[Category: | + | [[Category: Impch domain = alpha/beta/alpha]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:16:49 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:16, 2 May 2008
CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION
Overview
ATIC, 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.
About this Structure
1G8M is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 17:16:49 2008
