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1inl
From Proteopedia
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| - | [[ | + | ==Crystal Structure of Spermidine Synthase from Thermotoga Maritima== |
| + | <StructureSection load='1inl' size='340' side='right' caption='[[1inl]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1inl]] is a 4 chain structure with 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=1INL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1INL FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Spermidine_synthase Spermidine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.16 2.5.1.16] </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=1inl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1inl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1inl RCSB], [http://www.ebi.ac.uk/pdbsum/1inl PDBsum], [http://www.topsan.org/Proteins/MCSG/1inl TOPSAN]</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/in/1inl_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 == | ||
| + | Polyamines are essential in all branches of life. Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine. The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution in the presence and absence of AdoDATO (S-adenosyl-1,8-diamino-3-thiooctane), a compound containing both substrate and product moieties. This, the first structure of an aminopropyltransferase, reveals deep cavities for binding substrate and cofactor, and a loop that envelops the active site. The AdoDATO binding site is lined with residues conserved in PAPT enzymes from bacteria to humans, suggesting a universal catalytic mechanism. Other conserved residues act sterically to provide a structural basis for polyamine specificity. The enzyme is tetrameric; each monomer consists of a C-terminal domain with a Rossmann-like fold and an N-terminal beta-stranded domain. The tetramer is assembled using a novel barrel-type oligomerization motif. | ||
| - | + | The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor.,Korolev S, Ikeguchi Y, Skarina T, Beasley S, Arrowsmith C, Edwards A, Joachimiak A, Pegg AE, Savchenko A Nat Struct Biol. 2002 Jan;9(1):27-31. PMID:11731804<ref>PMID:11731804</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Spermidine Synthase|Spermidine Synthase]] | *[[Spermidine Synthase|Spermidine Synthase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Spermidine synthase]] | [[Category: Spermidine synthase]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
Revision as of 09:25, 28 September 2014
Crystal Structure of Spermidine Synthase from Thermotoga Maritima
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Categories: Spermidine synthase | Thermotoga maritima | Edwards, A. | Ikeguchi, Y. | Joachimiak, A. | Korolev, S. | MCSG, Midwest Center for Structural Genomics. | Pegg, A E. | Savchenko, A. | Skarina, T. | Beta-barrel | Mcsg | Midwest center for structural genomic | Protein structure initiative | Psi | Rossman fold | Structural genomic | Transferase

