View source for 4hl6


==YfdE from Escherichia coli==
<StructureSection load='4hl6' size='340' side='right'caption='[[4hl6]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hl6]] is a 6 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=4HL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HL6 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]] 2.12&#8491;</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=4hl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hl6 OCA], [https://pdbe.org/4hl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hl6 RCSB], [https://www.ebi.ac.uk/pdbsum/4hl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hl6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACOCT_ECOLI ACOCT_ECOLI] Involved in the catabolism of oxalate and in the adapatation to low pH. ACOCT serves to prime the oxalate-induced acid tolerance response (ATR) cycle by producing substrate for oxalyl-CoA decarboxylase (OXC) and formyl-coenzyme A transferase (FCOCT). Catalyzes the reversible conversion of acetyl-CoA and oxalate to oxalyl-CoA and acetate. It can also use formyl-CoA and oxalate to produce oxalyl-CoA and formate with significantly reduced specific activity.<ref>PMID:23935849</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many food plants accumulate oxalate, which humans absorb but do not metabolize, leading to the formation of urinary stones. The commensal bacterium Oxalobacter formigenes consumes oxalate by converting it to oxalyl-CoA, which is decarboxylated by oxalyl-CoA decarboxylase (OXC). OXC and the class III CoA-transferase formyl-CoA:oxalate CoA-transferase (FCOCT) are widespread among bacteria, including many that have no apparent ability to degrade or to resist external oxalate. The EvgA acid response regulator activates transcription of the Escherichia coli yfdXWUVE operon encoding YfdW (FCOCT), YfdU (OXC), and YfdE, a class III CoA-transferase that is [Formula: see text]30% identical to YfdW. YfdW and YfdU are necessary and sufficient for oxalate-induced protection against a subsequent acid challenge; neither of the other genes has a known function. We report the purification, in vitro characterization, 2.1-A crystal structure, and functional assignment of YfdE. YfdE and UctC, an orthologue from the obligate aerobe Acetobacter aceti, perform the reversible conversion of acetyl-CoA and oxalate to oxalyl-CoA and acetate. The annotation of YfdE as acetyl-CoA:oxalate CoA-transferase (ACOCT) expands the scope of metabolic pathways linked to oxalate catabolism and the oxalate-induced acid tolerance response. FCOCT and ACOCT active sites contain distinctive, conserved active site loops (the glycine-rich loop and the GNxH loop, respectively) that appear to encode substrate specificity.

Function and X-Ray crystal structure of Escherichia coli YfdE.,Mullins EA, Sullivan KL, Kappock TJ PLoS One. 2013 Jul 23;8(7):e67901. doi: 10.1371/journal.pone.0067901. Print 2013. PMID:23935849<ref>PMID:23935849</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hl6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Kappock TJ]]
[[Category: Mullins EA]]
[[Category: Nyffeler KE]]
[[Category: Sullivan KL]]