1l9x
From Proteopedia
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| - | [[Image:1l9x.jpg|left|200px]] | + | [[Image:1l9x.jpg|left|200px]] |
| - | + | ||
| - | '''Structure of gamma-Glutamyl Hydrolase''' | + | {{Structure |
| + | |PDB= 1l9x |SIZE=350|CAPTION= <scene name='initialview01'>1l9x</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Gamma-glutamyl_hydrolase Gamma-glutamyl hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.9 3.4.19.9] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of gamma-Glutamyl Hydrolase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L9X is a [ | + | 1L9X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9X OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11953431 11953431] |
[[Category: Gamma-glutamyl hydrolase]] | [[Category: Gamma-glutamyl hydrolase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: gamma-glutamyl hydrolase]] | [[Category: gamma-glutamyl hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:22 2008'' |
Revision as of 10:28, 20 March 2008
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| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Gamma-glutamyl hydrolase, with EC number 3.4.19.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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