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1poi

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[[Image:1poi.gif|left|200px]]<br /><applet load="1poi" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1poi, resolution 2.5&Aring;" />
 
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'''CRYSTAL STRUCTURE OF GLUTACONATE COENZYME A-TRANSFERASE FROM ACIDAMINOCOCCUS FERMENTANS TO 2.55 ANGSTOMS RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF GLUTACONATE COENZYME A-TRANSFERASE FROM ACIDAMINOCOCCUS FERMENTANS TO 2.55 ANGSTOMS RESOLUTION==
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BACKGROUND: Coenzyme A-transferases are a family of enzymes with a diverse substrate specificity and subunit composition. Members of this group of enzymes are found in anaerobic fermenting bacteria, aerobic bacteria and in the mitochondria of humans and other mammals, but so far none have been crystallized. A defect in the human gene encoding succinyl-CoA: 3-oxoacid CoA-transferase causes a metabolic disease which leads to severe ketoacidosis, thus reflecting the importance of this family of enzymes. All CoA-transferases share a common mechanism in which the CoA moiety is transferred from a donor (e.g. acetyl CoA) to an acceptor, (R)-2-hydroxyglutarate, whereby acetate is formed. The transfer has been described by a ping-pong mechanism in which CoA is bound to the active-site residue of the enzyme as a covalent thiol ester intermediate. We describe here the crystal structure of glutaconate CoA-transferase (GCT) from the strictly anaerobic bacterium Acidaminococcus fermentans. This enzyme activates (R)-2-hydroxyglutarate to (R)-2-hydroxyglutaryl-CoA in the pathway of glutamate fermentation. We initiated this project to gain further insight into the function of this enzyme and the structural basis for the characteristics of CoA-transferases. RESULTS: The crystal structure of GCT was solved by multiple isomorphous replacement to 2.55 A resolution. The enzyme is a heterooctamer and its overall arrangement of subunits can be regarded as an (AB)4tetramer obeying 222 symmetry. Both subunits A and B belong to the open alpha/beta-protein class and can be described as a four-layered alpha/alpha/beta/alpha type with a novel composition and connectivity of the secondary structure elements. The core of subunit A consists of seven alpha/beta repeats resulting in an all parallel central beta sheet, against which helices pack from both sides. In contrast, the centre of subunit B is formed by a ninefold mixed beta sheet. In both subunits the helical C terminus is folded back onto the N-terminal domain to form the third layer of helices. CONCLUSIONS: The active site of GCT is located at the interface of subunits A and B and is formed by loops of both subunits. The funnel-shaped opening to the active site has a depth and diameter of about 20 A with the catalytic residue, Glu54 of subunit B, at the bottom. The active-site glutamate residue is stabilized by hydrogen bonds. Despite very low amino acid sequence similarity, subunits A and B reveal a similar overall fold. Large parts of their structures can be spatially superimposed, suggesting that both subunits have evolved from a common ancestor.
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<StructureSection load='1poi' size='340' side='right'caption='[[1poi]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1poi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidaminococcus_fermentans Acidaminococcus fermentans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1POI FirstGlance]. <br>
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1POI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Acidaminococcus_fermentans Acidaminococcus fermentans] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POI OCA].
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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]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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==Reference==
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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=1poi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1poi OCA], [https://pdbe.org/1poi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1poi RCSB], [https://www.ebi.ac.uk/pdbsum/1poi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1poi ProSAT]</span></td></tr>
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Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases., Jacob U, Mack M, Clausen T, Huber R, Buckel W, Messerschmidt A, Structure. 1997 Mar 15;5(3):415-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9083111 9083111]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GCTA_ACIFV GCTA_ACIFV] Catalyzes the transfer of the CoA moiety from acetyl-CoA to (R)-2-hydroxyglutarate and related compounds like glutaconate.
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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/po/1poi_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=1poi ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Acidaminococcus fermentans]]
[[Category: Acidaminococcus fermentans]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Buckel, W.]]
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[[Category: Buckel W]]
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[[Category: Clausen, T.]]
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[[Category: Clausen T]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Jacob, U.]]
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[[Category: Jacob U]]
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[[Category: Mack, M.]]
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[[Category: Mack M]]
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[[Category: Messerschmidt, A.]]
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[[Category: Messerschmidt A]]
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[[Category: CU]]
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[[Category: coa]]
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[[Category: glutamate]]
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[[Category: protein fermentation]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:53 2008''
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Current revision

CRYSTAL STRUCTURE OF GLUTACONATE COENZYME A-TRANSFERASE FROM ACIDAMINOCOCCUS FERMENTANS TO 2.55 ANGSTOMS RESOLUTION

PDB ID 1poi

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