1p5h

<StructureSection load='1p5h' size='340' side='right' caption='[[1p5h]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1p5h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35274 Atcc 35274]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P5H FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p5r|1p5r]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=847 ATCC 35274])</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=1p5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5h OCA], [http://pdbe.org/1p5h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p5h RCSB], [http://www.ebi.ac.uk/pdbsum/1p5h PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/FCTA_OXAFO FCTA_OXAFO]] Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy.[HAMAP-Rule:MF_00742]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p5/1p5h_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Formyl-CoA transferase catalyses transfer of CoA from formate to oxalate in the first step of oxalate degradation by Oxalobacter formigenes, a bacterium present in the intestinal flora which is implicated in oxalate catabolism in mammals. Formyl-CoA transferase is a member of a family of CoA-transferases for which no structural information is available. We now report the three-dimensional structure of O.formigenes formyl-CoA transferase, which reveals a novel fold and a very striking assembly of the homodimer. The subunit is composed of a large and a small domain where residues from both the N- and C-termini of the subunit are part of the large domain. The linkers between the domains give the subunit a circular shape with a hole in the middle. The enzyme monomers are tightly interacting and are interlocked. This fold requires drastic rearrangement of approximately 75 residues at the C-terminus for formation of the dimer. The structure of a complex of formyl-CoA transferase with CoA is also reported and sets the scene for a mechanistic understanding of enzymes of this family of CoA-transferases.

Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer.,Ricagno S, Jonsson S, Richards N, Lindqvist Y EMBO J. 2003 Jul 1;22(13):3210-9. PMID:12839984<ref>PMID:12839984</ref>

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

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<div class="pdbe-citations 1p5h" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 35274]]

[[Category: Jonsson, S]]

[[Category: Lindqvist, Y]]

[[Category: Ricagno, S]]

[[Category: Richards, N]]

[[Category: Transferase]]