1kko

<table><tr><td colspan='2'>[[1kko]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25405 Atcc 25405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KKO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kkr|1kkr]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kko OCA], [http://pdbe.org/1kko PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kko RCSB], [http://www.ebi.ac.uk/pdbsum/1kko PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kko ProSAT]</span></td></tr>

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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1kko" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 25405]]

[[Category: Asano, Y]]

[[Category: Baker, P J]]

[[Category: Buckley, P A]]

[[Category: Kato, Y]]

[[Category: Levy, C W]]

[[Category: Rice, D W]]

[[Category: Sedelnikova, S]]

[[Category: Tim barrel]]