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| - | [[Image:1l9x.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1l9x| PDB=1l9x | SCENE= }} | | {{STRUCTURE_1l9x| PDB=1l9x | SCENE= }} |
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| - | '''Structure of gamma-Glutamyl Hydrolase'''
| + | ===Structure of gamma-Glutamyl Hydrolase=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11953431}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11953431 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11953431}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ryan, T J.]] | | [[Category: Ryan, T J.]] |
| | [[Category: Gamma-glutamyl hydrolase]] | | [[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 Wed Jul 2 12:04:07 2008'' |
Revision as of 09:04, 2 July 2008
Template:STRUCTURE 1l9x
Structure of gamma-Glutamyl Hydrolase
Template:ABSTRACT PUBMED 11953431
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 Wed Jul 2 12:04:07 2008
