1p5h: Difference between revisions

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==Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes==
==Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes==
<StructureSection load='1p5h' size='340' side='right' caption='[[1p5h]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1p5h' size='340' side='right'caption='[[1p5h]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p5r|1p5r]]</td></tr>
</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>
<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'>[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>
<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>
</table>
</table>
== Function ==
== Function ==
[[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]  
[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]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p5/1p5h_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p5/1p5h_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 1p5h" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Formyl-CoA transferase|Formyl-CoA transferase]]
*[[Formyl-CoA transferase|Formyl-CoA transferase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35274]]
[[Category: Large Structures]]
[[Category: Jonsson, S]]
[[Category: Oxalobacter formigenes]]
[[Category: Lindqvist, Y]]
[[Category: Jonsson S]]
[[Category: Ricagno, S]]
[[Category: Lindqvist Y]]
[[Category: Richards, N]]
[[Category: Ricagno S]]
[[Category: Caib-baif family]]
[[Category: Richards N]]
[[Category: Coa-transferase]]
[[Category: Intertwined]]
[[Category: Knotted fold]]
[[Category: Oxalate]]
[[Category: Oxalate degradation]]
[[Category: Transferase]]

Latest revision as of 11:05, 14 February 2024

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

Structural highlights

1p5h is a 2 chain structure with sequence from Oxalobacter formigenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1p5h, resolution 2.20Å

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