1p5h

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[[Image:1p5h.jpg|left|200px]]<br /><applet load="1p5h" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p5h, resolution 2.20&Aring;" />
 
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'''Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes'''<br />
 
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==Overview==
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==Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes==
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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.
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<StructureSection load='1p5h' size='340' side='right'caption='[[1p5h]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1p5h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1P5H FirstGlance]. <br>
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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]] 2.2&#8491;</td></tr>
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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=1p5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5h OCA], [https://pdbe.org/1p5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p5h RCSB], [https://www.ebi.ac.uk/pdbsum/1p5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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]
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== Evolutionary Conservation ==
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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/p5/1p5h_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=1p5h ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1P5H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5H OCA].
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*[[Formyl-CoA transferase|Formyl-CoA transferase]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12839984 12839984]
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[[Category: Large Structures]]
[[Category: Oxalobacter formigenes]]
[[Category: Oxalobacter formigenes]]
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[[Category: Single protein]]
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[[Category: Jonsson S]]
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[[Category: Jonsson, S.]]
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[[Category: Lindqvist Y]]
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[[Category: Lindqvist, Y.]]
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[[Category: Ricagno S]]
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[[Category: Ricagno, S.]]
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[[Category: Richards N]]
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[[Category: Richards, N.]]
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[[Category: caib-baif family]]
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[[Category: coa-transferase]]
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[[Category: intertwined]]
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[[Category: knotted fold]]
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[[Category: oxalate]]
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[[Category: oxalate degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:19 2008''
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Current revision

Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes

PDB ID 1p5h

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