3c8f

<StructureSection load='3c8f' size='340' side='right' caption='[[3c8f]], [[Resolution|resolution]] 2.25&Aring;' scene=''>

<table><tr><td colspan='2'>[[3c8f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C8F FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MT2:[(3S)-3-AMINO-3-CARBOXYPROPYL](ETHYL)METHYLSULFONIUM'>MT2</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Formate-C-acetyltransferase]-activating_enzyme [Formate-C-acetyltransferase]-activating enzyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.97.1.4 1.97.1.4] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c8f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c8f RCSB], [http://www.ebi.ac.uk/pdbsum/3c8f PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/PFLA_ECOLI PFLA_ECOLI]] Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/3c8f_consurf.spt"</scriptWhenChecked>

</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].

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== Publication Abstract from PubMed ==

Pyruvate formate-lyase activating enzyme generates a stable and catalytically essential glycyl radical on G(734) of pyruvate formate-lyase via the direct, stereospecific abstraction of a hydrogen atom from pyruvate formate-lyase. The activase performs this remarkable feat by using an iron-sulfur cluster and S-adenosylmethionine (AdoMet), thus placing it among the AdoMet radical superfamily of enzymes. We report here structures of the substrate-free and substrate-bound forms of pyruvate formate-lyase-activating enzyme, the first structures of an AdoMet radical activase. To obtain the substrate-bound structure, we have used a peptide substrate, the 7-mer RVSGYAV, which contains the sequence surrounding G(734). Our structures provide fundamental insights into the interactions between the activase and the G(734) loop of pyruvate formate-lyase and provide a structural basis for direct and stereospecific H atom abstraction from the buried G(734) of pyruvate formate-lyase.

Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme.,Vey JL, Yang J, Li M, Broderick WE, Broderick JB, Drennan CL Proc Natl Acad Sci U S A. 2008 Oct 21;105(42):16137-41. Epub 2008 Oct 13. PMID:18852451<ref>PMID:18852451</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Drennan, C L]]

[[Category: Vey, J L]]

[[Category: Activase]]

[[Category: Adomet radical]]

[[Category: Sam radical]]