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1q7l

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[[Image:1q7l.gif|left|200px]]<br /><applet load="1q7l" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1q7l.gif|left|200px]]
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caption="1q7l, resolution 1.40&Aring;" />
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'''Zn-binding domain of the T347G mutant of human aminoacylase-I'''<br />
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{{Structure
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|PDB= 1q7l |SIZE=350|CAPTION= <scene name='initialview01'>1q7l</scene>, resolution 1.40&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>
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|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]
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|GENE= ACY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Zn-binding domain of the T347G mutant of human aminoacylase-I'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Q7L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GLY:'>GLY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7L OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12933810 12933810]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:41 2008''
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''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


PDB ID 1q7l

Drag the structure with the mouse to rotate
, 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

Page seeded by OCA on Thu Mar 20 13:33:57 2008

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