1sbz
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1sbz.png|left|200px]] | ||
- | < | + | ==Crystal Structure of dodecameric FMN-dependent Ubix-like Decarboxylase from Escherichia coli O157:H7== |
- | + | <StructureSection load='1sbz' size='340' side='right'caption='[[1sbz]], [[Resolution|resolution]] 2.00Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1sbz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SBZ 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]] 2Å</td></tr> | |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1sbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sbz OCA], [https://pdbe.org/1sbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sbz RCSB], [https://www.ebi.ac.uk/pdbsum/1sbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sbz ProSAT], [https://www.topsan.org/Proteins/BSGI/1sbz TOPSAN]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/PADL_ECO57 PADL_ECO57] Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions (PubMed:15979273). Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase (By similarity).[HAMAP-Rule:MF_01986]<ref>PMID:15979273</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/sb/1sbz_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1sbz ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The crystal structure of the flavoprotein Pad1 from Escherichia coli O157:H7 complexed with the cofactor FMN has been determined by the multiple anomalous diffraction method and refined at 2.0 A resolution. This protein is a paralog of UbiX (3-octaprenyl-4-hydroxybenzoate carboxylyase, 51% sequence identity) that catalyzes the third step in ubiquinone biosynthesis and to Saccharomyces cerevisiae Pad1 (54% identity), an enzyme that confers resistance to the antimicrobial compounds phenylacrylic acids through decarboxylation of these compounds. Each Pad1 monomer consists of a typical Rossmann fold containing a non-covalently bound molecule of FMN. The fold of Pad1 is similar to MrsD, an enzyme associated with lantibiotic synthesis; EpiD, a peptidyl-cysteine decarboxylase; and AtHAL3a, the enzyme, which decarboxylates 4'-phosphopantothenoylcysteine to 4'-phosphopantetheine during coenzyme A biosynthesis, all with a similar location of the FMN binding site at the interface between two monomers, yet each having little sequence similarity to one another. All of these proteins associate into oligomers, with a trimer forming the common structural unit in each case. In MrsD and EpiD, which belong to the homo-dodecameric flavin-containing cysteine decarboxylase (HFCD) family, these trimers associate further into dodecamers. Pad1 also forms dodecamers, although the association of the trimers is completely different, resulting in exposure of a different side of the trimer unit to the solvent. This exposure affects the location of the substrate binding site and, specifically, its access to the FMN cofactor. Therefore, Pad1 forms a separate family, distinguishable from the HFCD family. | ||
- | + | Crystal structure of a dodecameric FMN-dependent UbiX-like decarboxylase (Pad1) from Escherichia coli O157: H7.,Rangarajan ES, Li Y, Iannuzzi P, Tocilj A, Hung LW, Matte A, Cygler M Protein Sci. 2004 Nov;13(11):3006-16. Epub 2004 Sep 30. PMID:15459342<ref>PMID:15459342</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1sbz" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Escherichia coli O157:H7]] |
- | + | [[Category: Large Structures]] | |
- | + | [[Category: Cygler M]] | |
- | == | + | [[Category: Hung L-W]] |
- | < | + | [[Category: Iannuzzi P]] |
- | [[Category: Escherichia coli]] | + | [[Category: Li Y]] |
- | [[Category: | + | [[Category: Matte A]] |
- | [[Category: Cygler | + | [[Category: Rangarajan ES]] |
- | [[Category: Hung | + | [[Category: Tocilj A]] |
- | [[Category: Iannuzzi | + | |
- | [[Category: Li | + | |
- | [[Category: Matte | + | |
- | [[Category: Rangarajan | + | |
- | [[Category: Tocilj | + | |
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Current revision
Crystal Structure of dodecameric FMN-dependent Ubix-like Decarboxylase from Escherichia coli O157:H7
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