1olt

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[[Image:1olt.jpg|left|200px]]
 
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==Coproporphyrinogen III oxidase (HemN) from Escherichia coli is a Radical SAM enzyme.==
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The line below this paragraph, containing "STRUCTURE_1olt", creates the "Structure Box" on the page.
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<StructureSection load='1olt' size='340' side='right'caption='[[1olt]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1olt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OLT FirstGlance]. <br>
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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]] 2.07&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
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{{STRUCTURE_1olt| PDB=1olt | SCENE= }}
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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=1olt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1olt OCA], [https://pdbe.org/1olt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1olt RCSB], [https://www.ebi.ac.uk/pdbsum/1olt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1olt ProSAT]</span></td></tr>
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</table>
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'''COPROPORPHYRINOGEN III OXIDASE (HEMN) FROM ESCHERICHIA COLI IS A RADICAL SAM ENZYME.'''
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== Function ==
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[https://www.uniprot.org/uniprot/HEMN_ECOLI HEMN_ECOLI] Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. It can use NAD or NADP, but NAD is preferred.<ref>PMID:7768836</ref> <ref>PMID:12114526</ref>
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== Evolutionary Conservation ==
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==Overview==
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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/ol/1olt_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=1olt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
'Radical SAM' enzymes generate catalytic radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. We present the first crystal structure of a Radical SAM enzyme, that of HemN, the Escherichia coli oxygen-independent coproporphyrinogen III oxidase, at 2.07 A resolution. HemN catalyzes the essential conversion of coproporphyrinogen III to protoporphyrinogen IX during heme biosynthesis. HemN binds a 4Fe-4S cluster through three cysteine residues conserved in all Radical SAM enzymes. A juxtaposed SAM coordinates the fourth Fe ion through its amide nitrogen and carboxylate oxygen. The SAM sulfonium sulfur is near both the Fe (3.5 A) and a neighboring sulfur of the cluster (3.6 A), allowing single electron transfer from the 4Fe-4S cluster to the SAM sulfonium. SAM is cleaved yielding a highly oxidizing 5'-deoxyadenosyl radical. HemN, strikingly, binds a second SAM immediately adjacent to the first. It may thus successively catalyze two propionate decarboxylations. The structure of HemN reveals the cofactor geometry required for Radical SAM catalysis and sets the stage for the development of inhibitors with antibacterial function due to the uniquely bacterial occurrence of the enzyme.
'Radical SAM' enzymes generate catalytic radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. We present the first crystal structure of a Radical SAM enzyme, that of HemN, the Escherichia coli oxygen-independent coproporphyrinogen III oxidase, at 2.07 A resolution. HemN catalyzes the essential conversion of coproporphyrinogen III to protoporphyrinogen IX during heme biosynthesis. HemN binds a 4Fe-4S cluster through three cysteine residues conserved in all Radical SAM enzymes. A juxtaposed SAM coordinates the fourth Fe ion through its amide nitrogen and carboxylate oxygen. The SAM sulfonium sulfur is near both the Fe (3.5 A) and a neighboring sulfur of the cluster (3.6 A), allowing single electron transfer from the 4Fe-4S cluster to the SAM sulfonium. SAM is cleaved yielding a highly oxidizing 5'-deoxyadenosyl radical. HemN, strikingly, binds a second SAM immediately adjacent to the first. It may thus successively catalyze two propionate decarboxylations. The structure of HemN reveals the cofactor geometry required for Radical SAM catalysis and sets the stage for the development of inhibitors with antibacterial function due to the uniquely bacterial occurrence of the enzyme.
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==About this Structure==
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Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes.,Layer G, Moser J, Heinz DW, Jahn D, Schubert WD EMBO J. 2003 Dec 1;22(23):6214-24. PMID:14633981<ref>PMID:14633981</ref>
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1OLT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLT OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes., Layer G, Moser J, Heinz DW, Jahn D, Schubert WD, EMBO J. 2003 Dec 1;22(23):6214-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14633981 14633981]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1olt" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Heinz, D W.]]
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<references/>
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[[Category: Jahn, D.]]
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__TOC__
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[[Category: Layer, G.]]
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</StructureSection>
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[[Category: Moser, J.]]
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[[Category: Escherichia coli K-12]]
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[[Category: Schubert, W D.]]
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[[Category: Large Structures]]
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[[Category: 4fe-4s cluster]]
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[[Category: Heinz DW]]
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[[Category: Decarboxylase]]
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[[Category: Jahn D]]
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[[Category: Heme biosynthesis]]
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[[Category: Layer G]]
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[[Category: Oxidoreductase]]
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[[Category: Moser J]]
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[[Category: Radical sam enzyme]]
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[[Category: Schubert W-D]]
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[[Category: S-adenosyl-l-methionine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:00:33 2008''
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Current revision

Coproporphyrinogen III oxidase (HemN) from Escherichia coli is a Radical SAM enzyme.

PDB ID 1olt

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