This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1l9x
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1l9x.jpg|left|200px]] | [[Image:1l9x.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1l9x", 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_1l9x| PDB=1l9x | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Structure of gamma-Glutamyl Hydrolase''' | '''Structure of gamma-Glutamyl Hydrolase''' | ||
| Line 30: | Line 27: | ||
[[Category: Roey, P Van.]] | [[Category: Roey, P Van.]] | ||
[[Category: Ryan, T J.]] | [[Category: Ryan, T J.]] | ||
| - | [[Category: | + | [[Category: Gamma-glutamyl hydrolase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:42:30 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:42, 2 May 2008
Structure of gamma-Glutamyl Hydrolase
Overview
gamma-Glutamyl hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. The crystal structure of human gamma-glutamyl hydrolase, determined at 1.6-A resolution, reveals that the protein is a homodimer. The overall structure of human gamma-glutamyl hydrolase contains 11 alpha-helices and 14 beta-strands, with a fold in which a central eight-stranded beta-sheet is sandwiched by three and five alpha-helices on each side. The topology is very similar to that of the class I glutamine amidotransferase domains, with the only major differences consisting of extensions in four loops and at the C terminus. These insertions are important for defining the substrate binding cleft and/or the dimer interface. Two sequence motifs are found in common between human gamma-glutamyl hydrolase and the class I glutamine amidotransferase family and include the catalytically essential residues, Cys-110 and His-220. These residues are located in the center of a large l-shaped cleft that is closed at one end and open at the other. Several conserved residues, including Glu-114, His-171, Gln-218, and Lys-223, may be important for substrate binding. Modeling of a methotrexate thioester intermediate, based on the corresponding complex of the glutamate thioester intermediate of Escherichia coli carbamoyl-phosphate synthetase, indicates that the substrate binds in an orientation with the pteroyl group toward the open end of the cleft.
About this Structure
1L9X is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate., Li H, Ryan TJ, Chave KJ, Van Roey P, J Biol Chem. 2002 Jul 5;277(27):24522-9. Epub 2002 Apr 12. PMID:11953431 Page seeded by OCA on Fri May 2 23:42:30 2008
