1q7l
From Proteopedia
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| - | [[Image:1q7l.gif|left|200px]] | + | [[Image:1q7l.gif|left|200px]] |
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| - | '''Zn-binding domain of the T347G mutant of human aminoacylase-I''' | + | {{Structure |
| + | |PDB= 1q7l |SIZE=350|CAPTION= <scene name='initialview01'>1q7l</scene>, resolution 1.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=GLY:GLYCINE'>GLY</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Aminoacylase Aminoacylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.14 3.5.1.14] | ||
| + | |GENE= ACY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Zn-binding domain of the T347G mutant of human aminoacylase-I''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Q7L is a [ | + | 1Q7L is a [[Protein complex]] structure of sequences 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=1Q7L OCA]. |
==Reference== | ==Reference== | ||
| - | Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family., Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Menard R, J Biol Chem. 2003 Nov 7;278(45):44496-504. Epub 2003 Aug 21. PMID:[http:// | + | Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family., Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Menard R, J Biol Chem. 2003 Nov 7;278(45):44496-504. Epub 2003 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12933810 12933810] |
[[Category: Aminoacylase]] | [[Category: Aminoacylase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''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 13:33:57 2008'' |
Revision as of 11:33, 20 March 2008
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| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | ACY1 (Homo sapiens) | ||||||
| Activity: | Aminoacylase, with EC number 3.5.1.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Zn-binding domain of the T347G mutant of human aminoacylase-I
Contents |
Overview
Members of the aminoacylase-1 (Acy1)/M20 family of aminoacylases and exopeptidases exist as either monomers or homodimers. They contain a zinc-binding domain and a second domain mediating dimerization in the latter case. The roles that both domains play in catalysis have been investigated for human Acy1 (hAcy1) by x-ray crystallography and by site-directed mutagenesis. Structure comparison of the dinuclear zinc center in a mutant of hAcy1 reported here with dizinc centers in related enzymes points to a difference in zinc ligation in the Acy1/M20 family. Mutational analysis supports catalytic roles of zinc ions, a vicinal glutamate, and a histidine from the dimerization domain. By complementing different active site mutants of hAcy1, we show that catalysis occurs at the dimer interface. Reinterpretation of the structure of a monomeric homolog, peptidase V, reveals that a domain insertion mimics dimerization. We conclude that monomeric and dimeric Acy1/M20 family members share a unique active site architecture involving both enzyme domains. The study may provide means to improve homologous carboxypeptidase G2 toward application in antibody-directed enzyme prodrug therapy.
Disease
Known disease associated with this structure: Aminoacylase 1 deficiency OMIM:[104620]
About this Structure
1Q7L is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family., Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Menard R, J Biol Chem. 2003 Nov 7;278(45):44496-504. Epub 2003 Aug 21. PMID:12933810
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