1kkr: Difference between revisions

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[[Image:1kkr.~~gif~~|left|200px]]

[[Image:1kkr.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE CONTAINING (2S,3S)-3-METHYLASPARTIC ACID~~'''~~

===CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE CONTAINING (2S,3S)-3-METHYLASPARTIC ACID===

~~==Overview==~~

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~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_11796115}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11796115 is the PubMed ID number.

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==About this Structure==

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[[Category: Substrate complex]]

[[Category: Tim barrel]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 22:51:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:29:06 2008''

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-[[Image:1kkr.gif|left|200px]]
+{{Seed}}
+[[Image:1kkr.png|left|200px]]
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 {{STRUCTURE_1kkr|  PDB=1kkr  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE CONTAINING (2S,3S)-3-METHYLASPARTIC ACID'''
+===CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE CONTAINING (2S,3S)-3-METHYLASPARTIC ACID===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11796115}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11796115 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11796115}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Substrate complex]]
 [[Category: Tim barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:51:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:29:06 2008''