1h18

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[[Image:1h18.jpg|left|200px]]
 
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==Pyruvate Formate-Lyase (E.coli) in complex with Pyruvate==
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The line below this paragraph, containing "STRUCTURE_1h18", creates the "Structure Box" on the page.
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<StructureSection load='1h18' size='340' side='right'caption='[[1h18]], [[Resolution|resolution]] 2.30&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'>[[1h18]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H18 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.3&#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=DTL:L-TREITOL'>DTL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
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{{STRUCTURE_1h18| PDB=1h18 | 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=1h18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h18 OCA], [https://pdbe.org/1h18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h18 RCSB], [https://www.ebi.ac.uk/pdbsum/1h18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h18 ProSAT]</span></td></tr>
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</table>
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'''PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH PYRUVATE'''
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== Function ==
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[https://www.uniprot.org/uniprot/PFLB_ECOLI PFLB_ECOLI]
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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/h1/1h18_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=1h18 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 ==
The glycyl radical enzyme pyruvate formate-lyase (PFL) synthesizes acetyl-CoA and formate from pyruvate and CoA. With the crystal structure of the non-radical form of PFL in complex with its two substrates, we have trapped the moment prior to pyruvate cleavage. The structure reveals how the active site aligns the scissile bond of pyruvate for radical attack, prevents non-radical side reactions of the pyruvate, and confines radical migration. The structure shows CoA in a syn conformation awaiting pyruvate cleavage. By changing to an anti conformation, without affecting the adenine binding mode of CoA, the thiol of CoA could pick up the acetyl group resulting from pyruvate cleavage.
The glycyl radical enzyme pyruvate formate-lyase (PFL) synthesizes acetyl-CoA and formate from pyruvate and CoA. With the crystal structure of the non-radical form of PFL in complex with its two substrates, we have trapped the moment prior to pyruvate cleavage. The structure reveals how the active site aligns the scissile bond of pyruvate for radical attack, prevents non-radical side reactions of the pyruvate, and confines radical migration. The structure shows CoA in a syn conformation awaiting pyruvate cleavage. By changing to an anti conformation, without affecting the adenine binding mode of CoA, the thiol of CoA could pick up the acetyl group resulting from pyruvate cleavage.
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==About this Structure==
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X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage.,Becker A, Kabsch W J Biol Chem. 2002 Oct 18;277(42):40036-42. Epub 2002 Aug 5. PMID:12163496<ref>PMID:12163496</ref>
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1H18 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=1H18 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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X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage., Becker A, Kabsch W, J Biol Chem. 2002 Oct 18;277(42):40036-42. Epub 2002 Aug 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12163496 12163496]
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</div>
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<div class="pdbe-citations 1h18" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Formate C-acetyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Becker A]]
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[[Category: Becker, A.]]
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[[Category: Kabsch W]]
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[[Category: Kabsch, W.]]
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[[Category: Acetylation]]
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[[Category: Acyltransferase]]
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[[Category: Glycyl radical enzyme]]
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[[Category: Lyase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:17:20 2008''
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Current revision

Pyruvate Formate-Lyase (E.coli) in complex with Pyruvate

PDB ID 1h18

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