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1l9x

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[[Image:1l9x.jpg|left|200px]]
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{{STRUCTURE_1l9x| PDB=1l9x | SCENE= }}
{{STRUCTURE_1l9x| PDB=1l9x | SCENE= }}
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'''Structure of gamma-Glutamyl Hydrolase'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11953431 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11953431}}
==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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:42:30 2008''
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''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

Image:1l9x.png

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

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