1p5h: Difference between revisions

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[[Image:1p5h.jpg|left|200px]]


{{Structure
==Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes==
|PDB= 1p5h |SIZE=350|CAPTION= <scene name='initialview01'>1p5h</scene>, resolution 2.20&Aring;
<StructureSection load='1p5h' size='340' side='right'caption='[[1p5h]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY=  
</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>
|GENE= FRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=847 Oxalobacter formigenes])
<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>
}}
</table>
== Function ==
[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 ==
[[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/p5/1p5h_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/main_output.php?pdb_ID=1p5h ConSurf].
<div style="clear:both"></div>


'''Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes'''
==See Also==
 
*[[Formyl-CoA transferase|Formyl-CoA transferase]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1P5H is a [[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].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/12839984 12839984]
[[Category: Oxalobacter formigenes]]
[[Category: Oxalobacter formigenes]]
[[Category: Single protein]]
[[Category: Jonsson S]]
[[Category: Jonsson, S.]]
[[Category: Lindqvist Y]]
[[Category: Lindqvist, Y.]]
[[Category: Ricagno S]]
[[Category: Ricagno, S.]]
[[Category: Richards N]]
[[Category: Richards, N.]]
[[Category: caib-baif family]]
[[Category: coa-transferase]]
[[Category: intertwined]]
[[Category: knotted fold]]
[[Category: oxalate]]
[[Category: oxalate degradation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:20:10 2008''

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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