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New page: left|200px<br /><applet load="1on3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1on3, resolution 1.90Å" /> '''Transcarboxylase 12S...
 
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[[Image:1on3.jpg|left|200px]]<br /><applet load="1on3" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1on3, resolution 1.90&Aring;" />
'''Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)'''<br />


==Overview==
==Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)==
Transcarboxylase from Propionibacterium shermanii is a 1.2 MDa multienzyme, complex that couples two carboxylation reactions, transferring CO(2)(-), from methylmalonyl-CoA to pyruvate, yielding propionyl-CoA and, oxaloacetate. The 1.9 A resolution crystal structure of the central 12S, hexameric core, which catalyzes the first carboxylation reaction, has been, solved bound to its substrate methylmalonyl-CoA. Overall, the structure, reveals two stacked trimers related by 2-fold symmetry, and a domain, duplication in the monomer. In the active site, the labile carboxylate, group of methylmalonyl-CoA is stabilized by interaction with the N-termini, of two alpha-helices. The 12S domains are structurally similar to the, crotonase/isomerase superfamily, although only domain 1 of each 12S, monomer binds ligand. The 12S reaction is similar to that of human, propionyl-CoA carboxylase, whose beta-subunit has 50% sequence identity, with 12S. A homology model of the propionyl-CoA carboxylase beta-subunit, based on this 12S crystal structure, provides new insight into the, propionyl-CoA carboxylase mechanism, its oligomeric structure and the, molecular basis of mutations responsible for enzyme deficiency in, propionic acidemia.
<StructureSection load='1on3' size='340' side='right'caption='[[1on3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1on3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii Propionibacterium freudenreichii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ON3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ON3 FirstGlance]. <br>
1ON3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii Propionibacterium freudenreichii] with CD, MCA, DXX and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ON3 OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=DXX:METHYLMALONIC+ACID'>DXX</scene>, <scene name='pdbligand=MCA:METHYLMALONYL-COENZYME+A'>MCA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1on3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1on3 OCA], [https://pdbe.org/1on3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1on3 RCSB], [https://www.ebi.ac.uk/pdbsum/1on3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1on3 ProSAT]</span></td></tr>
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core., Hall PR, Wang YF, Rivera-Hainaj RE, Zheng X, Pustai-Carey M, Carey PR, Yee VC, EMBO J. 2003 May 15;22(10):2334-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12743028 12743028]
</table>
[[Category: Methylmalonyl-CoA carboxytransferase]]
== Function ==
[https://www.uniprot.org/uniprot/12S_PROFR 12S_PROFR] The 12S subunit specifically catalyzes the transfer of the carboxyl group of methylmalonyl CoA to the biotin of the 1.3S subunit forming propanoyl-CoA and carboxylated 1.3S-biotin.
== 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/on/1on3_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=1on3 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Propionibacterium freudenreichii]]
[[Category: Propionibacterium freudenreichii]]
[[Category: Single protein]]
[[Category: Carey PR]]
[[Category: Carey, P.R.]]
[[Category: Hall PR]]
[[Category: Hall, P.R.]]
[[Category: Pustai-Carey M]]
[[Category: Pustai-Carey, M.]]
[[Category: Rivera-Hainaj RE]]
[[Category: Rivera-Hainaj, R.E.]]
[[Category: Wang Y-F]]
[[Category: Wang, Y.F.]]
[[Category: Yee VC]]
[[Category: Yee, V.C.]]
[[Category: Zheng X]]
[[Category: Zheng, X.]]
[[Category: CD]]
[[Category: DXX]]
[[Category: MCA]]
[[Category: MPD]]
[[Category: carboxyl transferase]]
[[Category: crystal structure]]
[[Category: domain duplication]]
[[Category: multienzyme complex]]
[[Category: transcarboxylase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:01:32 2007''

Latest revision as of 08:01, 14 February 2024

Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)

1on3, resolution 1.90Å

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