1kko: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 3: Line 3:
<StructureSection load='1kko' size='340' side='right'caption='[[1kko]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
<StructureSection load='1kko' size='340' side='right'caption='[[1kko]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[1kko]] 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=1KKO OCA]. For a <b>guided tour on the structure components</b> use [https://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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.33&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kko OCA], [https://pdbe.org/1kko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kko RCSB], [https://www.ebi.ac.uk/pdbsum/1kko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kko ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35703 ATCC 25405])</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>
</table>
</table>
== 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 21: Line 20:
</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=1kko ConSurf].
</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=1kko ConSurf].
<div style="clear:both"></div>
<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.
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>
</div>
<div class="pdbe-citations 1kko" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 25405]]
[[Category: Citrobacter amalonaticus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Methylaspartate ammonia-lyase]]
[[Category: Asano Y]]
[[Category: Asano, Y]]
[[Category: Baker PJ]]
[[Category: Baker, P J]]
[[Category: Buckley PA]]
[[Category: Buckley, P A]]
[[Category: Kato Y]]
[[Category: Kato, Y]]
[[Category: Levy CW]]
[[Category: Levy, C W]]
[[Category: Rice DW]]
[[Category: Rice, D W]]
[[Category: Sedelnikova S]]
[[Category: Sedelnikova, S]]
[[Category: Enolase superfamily]]
[[Category: Lyase]]
[[Category: Methylaspartate ammonia lyase]]
[[Category: Tim barrel]]

Revision as of 08:01, 3 April 2024

CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE

1kko, resolution 1.33Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1kko&oldid=4121713"