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[[Image:1mhm.png|left|200px]]
==Crystal structure of S-adenosylmethionine decarboxylase from potato==
<StructureSection load='1mhm' size='340' side='right' caption='[[1mhm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mhm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MHM FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jen|1jen]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylmethionine_decarboxylase Adenosylmethionine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.50 4.1.1.50] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mhm RCSB], [http://www.ebi.ac.uk/pdbsum/1mhm PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[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/mh/1mhm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
S-Adenosylmethionine decarboxylase has been implicated in cell growth and differentiation and is synthesized as a proenzyme, which undergoes autocatalytic cleavage to generate an active site pyruvoyl group. In mammals, S-adenosylmethionine decarboxylase is active as a dimer in which each protomer contains one alpha subunit and one beta subunit. In many higher organisms, autocatalysis and decarboxylation are stimulated by putrescine, which binds in a buried site containing numerous negatively charged residues. In contrast, plant S-adenosylmethionine decarboxylases are fully active in the absence of putrescine, with rapid autocatalysis that is not stimulated by putrescine. We have determined the structure of the S-adenosylmethionine decarboxylase from potato, Solanum tuberosum, to 2.3 A resolution. Unlike the previously determined human enzyme structure, the potato enzyme is a monomer in the crystal structure. Ultracentrifugation studies show that the potato enzyme is also a monomer under physiological conditions, with a weak self-association constant of 6.5 x 10(4) M(-)(1) for the monomer-dimer association. Although the potato enzyme contains most of the buried charged residues that make up the putrescine binding site in the human enzyme, there is no evidence for a putrescine binding site in the potato enzyme. Instead, several amino acid substitutions, including Leu13/Arg18, Phe111/Arg114, Asp174/Val181, and Phe285/His294 (human/potato), provide side chains that mimic the role of putrescine in the human enzyme. In the potato enzyme, the positively charged residues form an extensive network of hydrogen bonds bridging a cluster of highly conserved negatively charged residues and the active site, including interactions with the catalytic residues Glu16 and His249. The results explain the constitutively high activity of plant S-adenosylmethionine decarboxylases in the absence of putrescine and are consistent with previously proposed models for how putrescine together with the buried, negatively charged site regulates enzyme activity.


{{STRUCTURE_1mhm|  PDB=1mhm  |  SCENE=  }}
Monomeric S-adenosylmethionine decarboxylase from plants provides an alternative to putrescine stimulation.,Bennett EM, Ekstrom JL, Pegg AE, Ealick SE Biochemistry. 2002 Dec 10;41(49):14509-17. PMID:12463749<ref>PMID:12463749</ref>


===Crystal structure of S-adenosylmethionine decarboxylase from potato===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_12463749}}
 
==About this Structure==
[[1mhm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHM OCA].


==See Also==
==See Also==
*[[S-adenosylmethionine decarboxylase|S-adenosylmethionine decarboxylase]]
*[[SAM decarboxylase|SAM decarboxylase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:012463749</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Adenosylmethionine decarboxylase]]
[[Category: Adenosylmethionine decarboxylase]]
[[Category: Solanum tuberosum]]
[[Category: Solanum tuberosum]]
Retrieved from "https://proteopedia.org/1mhm"