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


{{Structure
==CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE CONTAINING (2S,3S)-3-METHYLASPARTIC ACID==
|PDB= 1kkr |SIZE=350|CAPTION= <scene name='initialview01'>1kkr</scene>, resolution 2.10&Aring;
<StructureSection load='1kkr' size='340' side='right'caption='[[1kkr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=3MD:2S,3S-3-METHYLASPARTIC ACID'>3MD</scene>
<table><tr><td colspan='2'>[[1kkr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_amalonaticus Citrobacter amalonaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KKR FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
|GENE= MAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35703 Citrobacter amalonaticus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AS:(2S,3S)-3-METHYL-ASPARTIC+ACID'>2AS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kkr OCA], [https://pdbe.org/1kkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kkr RCSB], [https://www.ebi.ac.uk/pdbsum/1kkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kkr ProSAT]</span></td></tr>
 
</table>
'''CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE CONTAINING (2S,3S)-3-METHYLASPARTIC ACID'''
== Function ==
 
[https://www.uniprot.org/uniprot/MAAL_CITAM MAAL_CITAM] Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate (By similarity).
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kk/1kkr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kkr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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==
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<ref>PMID:11796115</ref>
1KKR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_amalonaticus Citrobacter amalonaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKR OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://www.ncbi.nlm.nih.gov/pubmed/11796115 11796115]
</div>
<div class="pdbe-citations 1kkr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Citrobacter amalonaticus]]
[[Category: Citrobacter amalonaticus]]
[[Category: Methylaspartate ammonia-lyase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Asano Y]]
[[Category: Asano, Y.]]
[[Category: Baker PJ]]
[[Category: Baker, P J.]]
[[Category: Buckley PA]]
[[Category: Buckley, P A.]]
[[Category: Kato K]]
[[Category: Kato, K.]]
[[Category: Levy CW]]
[[Category: Levy, C W.]]
[[Category: Rice DW]]
[[Category: Rice, D W.]]
[[Category: Sedelnikova S]]
[[Category: Sedelnikova, S.]]
[[Category: 3MD]]
[[Category: MG]]
[[Category: enolase superfamily]]
[[Category: methylaspartate ammonia lyase]]
[[Category: substrate complex]]
[[Category: tim barrel]]
 
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Retrieved from "https://proteopedia.org/1kkr"