1auk
From Proteopedia
(New page: 200px<br /> <applet load="1auk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1auk, resolution 2.1Å" /> '''HUMAN ARYLSULFATASE ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1AUK is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with MG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.6.8 3.1.6.8]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AUK OCA]]. | + | 1AUK is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with MG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Cerebroside-sulfatase Cerebroside-sulfatase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.6.8 3.1.6.8]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AUK OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis., Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W, Biochemistry. 1998 Mar 17;37(11):3654-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9521684 9521684] | Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis., Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W, Biochemistry. 1998 Mar 17;37(11):3654-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9521684 9521684] | ||
| + | [[Category: Cerebroside-sulfatase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lysosomal enzyme]] | [[Category: lysosomal enzyme]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:48:06 2007'' |
Revision as of 11:43, 30 October 2007
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HUMAN ARYLSULFATASE A
Overview
Human lysosomal arylsulfatase A (ASA) is a prototype member of the, sulfatase family. These enzymes require the posttranslational oxidation of, the -CH2SH group of a conserved cysteine to an aldehyde, yielding a, formylglycine. Without this modification sulfatases are catalytically, inactive, as revealed by a lysosomal storage disorder known as multiple, sulfatase deficiency. The 2.1 A resolution X-ray crystal structure shows, an ASA homooctamer composed of a tetramer of dimers, (alpha 2)4. The, alpha/beta fold of the monomer has significant structural analogy to, another hydrolytic enzyme, the alkaline phosphatase, and superposition of, these two structures shows that the active centers are located in largely, identical positions. The functionally essential formylglycine is located, in a ... [(full description)]
About this Structure
1AUK is a [Single protein] structure of sequence from [Homo sapiens] with MG as [ligand]. Active as [Cerebroside-sulfatase], with EC number [3.1.6.8]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis., Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W, Biochemistry. 1998 Mar 17;37(11):3654-64. PMID:9521684
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