3o4f
From Proteopedia
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| - | [[Image:3o4f.png|left|200px]] | ||
| - | + | ==Crystal Structure of Spermidine Synthase from E. coli== | |
| + | <StructureSection load='3o4f' size='340' side='right'caption='[[3o4f]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3o4f]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3adn 3adn] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3hh9 3hh9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O4F FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o4f OCA], [https://pdbe.org/3o4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o4f RCSB], [https://www.ebi.ac.uk/pdbsum/3o4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o4f ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SPEE_ECOLI SPEE_ECOLI] Involved in the biosynthesis of polyamines which play a significant role in the structural and functional organization in the chromoid of E.coli by compacting DNA and neutralizing negative charges. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. Cadaverine (1,5-diaminopentane) and spermidine can replace putrescine as the propylamine acceptor.<ref>PMID:23001854</ref> <ref>PMID:4572733</ref> | ||
| + | == 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/o4/3o4f_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/main_output.php?pdb_ID=3o4f ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Polyamines are essential in all branches of life. Biosynthesis of spermidine, one of the most ubiquitous polyamines, is catalyzed by spermidine synthase (SpeE). Although the function of this enzyme from Escherichia coli has been thoroughly characterised, its structural details remain unknown. Here, we report the crystal structure of E. coli SpeE and study its interaction with the ligands by isothermal titration calorimetry and computational modelling. SpeE consists of two domains - a small N-terminal beta-strand domain, and a C-terminal catalytic domain that adopts a canonical methyltransferase (MTase) Rossmann fold. The protein forms a dimer in the crystal and in solution. Structural comparison of E. coli SpeE to its homologs reveals that it has a large and unique substrate-binding cleft that may account for its lower amine substrate specificity. | ||
| - | + | The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket.,Zhou X, Chua TK, Tkaczuk KL, Bujnicki JM, Sivaraman J J Struct Biol. 2010 Mar;169(3):277-85. Epub 2010 Jan 4. PMID:20051267<ref>PMID:20051267</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3o4f" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
| - | *[[Spermidine | + | *[[Spermidine synthase 3D structures|Spermidine synthase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: Escherichia coli]] | + | </StructureSection> |
| - | [[Category: | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Chruszcz | + | [[Category: Large Structures]] |
| - | [[Category: Chua | + | [[Category: Chruszcz M]] |
| - | [[Category: Minor | + | [[Category: Chua TK]] |
| - | [[Category: Sivaraman | + | [[Category: Minor W]] |
| - | [[Category: Tkaczuk | + | [[Category: Sivaraman J]] |
| - | [[Category: Zhou | + | [[Category: Tkaczuk KL]] |
| - | + | [[Category: Zhou X]] | |
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Current revision
Crystal Structure of Spermidine Synthase from E. coli
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