3pfl: Difference between revisions
m Protected "3pfl" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF PFL FROM E.COLI IN COMPLEX WITH SUBSTRATE ANALOGUE OXAMATE== | |||
<StructureSection load='3pfl' size='340' side='right' caption='[[3pfl]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pfl]] is a 2 chain structure with 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=3PFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PFL FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OXM:OXAMIC+ACID'>OXM</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 Formate C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.54 2.3.1.54] </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=3pfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pfl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pfl RCSB], [http://www.ebi.ac.uk/pdbsum/3pfl PDBsum]</span></td></tr> | |||
</table> | |||
== 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/pf/3pfl_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pyruvate formate-lyase (PFL) from Escherichia coli uses a radical mechanism to reversibly cleave the C1-C2 bond of pyruvate using the Gly 734 radical and two cysteine residues (Cys 418, Cys 419). We have determined by X-ray crystallography the structures of PFL (non-radical form), its complex with the substrate analog oxamate, and the C418A,C419A double mutant. The atomic model (a dimer of 759-residue monomers) comprises a 10-stranded beta/alpha barrel assembled in an antiparallel manner from two parallel five-stranded beta-sheets; this architecture resembles that of ribonucleotide reductases. Gly 734 and Cys 419, positioned at the tips of opposing hairpin loops, meet in the apolar barrel center (Calpha-Sgamma = 3.7 A). Oxamate fits into a compact pocket where C2 is juxtaposed with Cys 418Sgamma (3.3 A), which in turn is close to Cys 419Sgamma (3.7 A). Our model of the active site is suggestive of a snapshot of the catalytic cycle, when the pyruvate-carbonyl awaits attack by the Cys 418 thiyl radical. We propose a homolytic radical mechanism for PFL that involves Cys 418 and Cys 419 both as thiyl radicals, with distinct chemical functions. | |||
Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase.,Becker A, Fritz-Wolf K, Kabsch W, Knappe J, Schultz S, Volker Wagner AF Nat Struct Biol. 1999 Oct;6(10):969-75. PMID:10504733<ref>PMID:10504733</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Formate C-acetyltransferase]] | [[Category: Formate C-acetyltransferase]] | ||
[[Category: Becker, A | [[Category: Becker, A]] | ||
[[Category: Fritz-Wolf, K | [[Category: Fritz-Wolf, K]] | ||
[[Category: Kabsch, W | [[Category: Kabsch, W]] | ||
[[Category: Knappe, J | [[Category: Knappe, J]] | ||
[[Category: Schultz, S | [[Category: Schultz, S]] | ||
[[Category: Wagner, A F.V | [[Category: Wagner, A F.V]] | ||
[[Category: Glucose metabolism]] | [[Category: Glucose metabolism]] | ||
[[Category: Glycyl radical enzyme]] | [[Category: Glycyl radical enzyme]] | ||
[[Category: Lyase-transferase complex]] | [[Category: Lyase-transferase complex]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||