1p5h: Difference between revisions

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New page: left|200px<br /><applet load="1p5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p5h, resolution 2.20Å" /> '''Crystal structure of...
 
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[[Image:1p5h.jpg|left|200px]]<br /><applet load="1p5h" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes'''<br />


==Overview==
==Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes==
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.
<StructureSection load='1p5h' size='340' side='right'caption='[[1p5h]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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='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='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>


==About this Structure==
==See Also==
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P5H OCA].
*[[Formyl-CoA transferase|Formyl-CoA transferase]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Large Structures]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:29:27 2007''

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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