1q7l
From Proteopedia
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|PDB= 1q7l |SIZE=350|CAPTION= <scene name='initialview01'>1q7l</scene>, resolution 1.40Å | |PDB= 1q7l |SIZE=350|CAPTION= <scene name='initialview01'>1q7l</scene>, resolution 1.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= ACY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ACY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7l OCA], [http://www.ebi.ac.uk/pdbsum/1q7l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q7l RCSB]</span> | ||
}} | }} | ||
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[[Category: Lunin, V V.]] | [[Category: Lunin, V V.]] | ||
[[Category: Menard, R.]] | [[Category: Menard, R.]] | ||
| - | [[Category: GLY]] | ||
| - | [[Category: ZN]] | ||
[[Category: aminoacylase-1]] | [[Category: aminoacylase-1]] | ||
[[Category: catalysis]] | [[Category: catalysis]] | ||
| Line 41: | Line 42: | ||
[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:09:53 2008'' |
Revision as of 20:09, 30 March 2008
| |||||||
| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ACY1 (Homo sapiens) | ||||||
| Activity: | Aminoacylase, with EC number 3.5.1.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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