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1tmi

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[[Image:1tmi.gif|left|200px]]
 
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{{Structure
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==Structure of Thermotoga maritima S63A non-processing mutant S-adenosylmethionine decarboxylase==
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|PDB= 1tmi |SIZE=350|CAPTION= <scene name='initialview01'>1tmi</scene>, resolution 1.70&Aring;
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<StructureSection load='1tmi' size='340' side='right'caption='[[1tmi]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1tmi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TMI FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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|GENE= SPEH, TM0655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tmi OCA], [https://pdbe.org/1tmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tmi RCSB], [https://www.ebi.ac.uk/pdbsum/1tmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tmi ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1tlu|1TLU]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tmi OCA], [http://www.ebi.ac.uk/pdbsum/1tmi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tmi RCSB]</span>
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[https://www.uniprot.org/uniprot/SPEH_THEMA SPEH_THEMA]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tm/1tmi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1tmi ConSurf].
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<div style="clear:both"></div>
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'''Structure of Thermotoga maritima S63A non-processing mutant S-adenosylmethionine decarboxylase'''
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==See Also==
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*[[SAM decarboxylase|SAM decarboxylase]]
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__TOC__
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==Overview==
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</StructureSection>
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S-adenosylmethionine decarboxylase (AdoMetDC) is a critical regulatory enzyme of the polyamine biosynthetic pathway and belongs to a small class of pyruvoyl-dependent amino acid decarboxylases. Structural elucidation of the prokaryotic AdoMetDC is of substantial interest in order to determine the relationship between the eukaryotic and prokaryotic forms of the enzyme. Although both forms utilize pyruvoyl groups, there is no detectable sequence similarity except at the site of pyruvoyl group formation. The x-ray structure of the Thermatoga maritima AdoMetDC proenzyme reveals a dimeric protein fold that is remarkably similar to the eukaryotic AdoMetDC protomer, suggesting an evolutionary link between the two forms of the enzyme. Three key active site residues (Ser55, His68, and Cys83) involved in substrate binding, catalysis or proenzyme processing that were identified in the human and potato AdoMet-DCs are structurally conserved in the T. maritima AdoMetDC despite very limited primary sequence identity. The role of Ser55, His68, and Cys83 in the self-processing reaction was investigated through site-directed mutagenesis. A homology model for the Escherichia coli AdoMetDC was generated based on the structures of the T. maritima and human AdoMetDCs.
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[[Category: Large Structures]]
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==About this Structure==
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1TMI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TMI OCA].
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==Reference==
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Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase., Toms AV, Kinsland C, McCloskey DE, Pegg AE, Ealick SE, J Biol Chem. 2004 Aug 6;279(32):33837-46. Epub 2004 May 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15150268 15150268]
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[[Category: Adenosylmethionine decarboxylase]]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Ealick, S E.]]
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[[Category: Ealick SE]]
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[[Category: Kinsland, C.]]
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[[Category: Kinsland C]]
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[[Category: McCloskey, D E.]]
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[[Category: McCloskey DE]]
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[[Category: Pegg, A E.]]
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[[Category: Pegg AE]]
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[[Category: Toms, A V.]]
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[[Category: Toms AV]]
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[[Category: two-layer alpha beta-sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:58:08 2008''
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Current revision

Structure of Thermotoga maritima S63A non-processing mutant S-adenosylmethionine decarboxylase

PDB ID 1tmi

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