1kko
From Proteopedia
(New page: 200px<br /><applet load="1kko" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kko, resolution 1.33Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1kko.gif|left|200px]]<br /><applet load="1kko" size=" | + | [[Image:1kko.gif|left|200px]]<br /><applet load="1kko" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kko, resolution 1.33Å" /> | caption="1kko, resolution 1.33Å" /> | ||
'''CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE'''<br /> | '''CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Methylaspartate ammonia lyase (MAL) catalyzes the magnesium-dependent | + | Methylaspartate ammonia lyase (MAL) catalyzes the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. The 1.3 A MAD crystal structure of the dimeric Citrobacter amalonaticus MAL shows that each subunit comprises two domains, one of which adopts the classical TIM barrel fold, with the active site at the C-terminal end of the barrel. Despite very low sequence similarity, the structure of MAL is closely related to those of representative members of the enolase superfamily, indicating that the mechanism of MAL involves the initial abstraction of a proton alpha to the 3-carboxyl of (2S,3S)-3-methylasparic acid to yield an enolic intermediate. This analysis resolves the conflict that had linked MAL to the histidine and phenylalanine ammonia lyase family of enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1KKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_amalonaticus Citrobacter amalonaticus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methylaspartate_ammonia-lyase Methylaspartate ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.2 4.3.1.2] Full crystallographic information is available from [http:// | + | 1KKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_amalonaticus Citrobacter amalonaticus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methylaspartate_ammonia-lyase Methylaspartate ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.2 4.3.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Asano, Y.]] | [[Category: Asano, Y.]] | ||
| - | [[Category: Baker, P | + | [[Category: Baker, P J.]] |
| - | [[Category: Buckley, P | + | [[Category: Buckley, P A.]] |
[[Category: Kato, Y.]] | [[Category: Kato, Y.]] | ||
| - | [[Category: Levy, C | + | [[Category: Levy, C W.]] |
| - | [[Category: Rice, D | + | [[Category: Rice, D W.]] |
[[Category: Sedelnikova, S.]] | [[Category: Sedelnikova, S.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:11 2008'' |
Revision as of 11:35, 21 February 2008
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CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE
Overview
Methylaspartate ammonia lyase (MAL) catalyzes the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. The 1.3 A MAD crystal structure of the dimeric Citrobacter amalonaticus MAL shows that each subunit comprises two domains, one of which adopts the classical TIM barrel fold, with the active site at the C-terminal end of the barrel. Despite very low sequence similarity, the structure of MAL is closely related to those of representative members of the enolase superfamily, indicating that the mechanism of MAL involves the initial abstraction of a proton alpha to the 3-carboxyl of (2S,3S)-3-methylasparic acid to yield an enolic intermediate. This analysis resolves the conflict that had linked MAL to the histidine and phenylalanine ammonia lyase family of enzymes.
About this Structure
1KKO is a Single protein structure of sequence from Citrobacter amalonaticus with as ligand. Active as Methylaspartate ammonia-lyase, with EC number 4.3.1.2 Full crystallographic information is available from OCA.
Reference
Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase., Levy CW, Buckley PA, Sedelnikova S, Kato Y, Asano Y, Rice DW, Baker PJ, Structure. 2002 Jan;10(1):105-13. PMID:11796115
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