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| | ==Crystal structure of the Apc core complex== | | ==Crystal structure of the Apc core complex== |
| - | <StructureSection load='5l9w' size='340' side='right' caption='[[5l9w]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='5l9w' size='340' side='right'caption='[[5l9w]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l9w]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aromatoleum_aromaticum_(strain_ebn1) Aromatoleum aromaticum (strain ebn1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L9W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L9W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l9w]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aromatoleum_aromaticum_(strain_ebn1) Aromatoleum aromaticum (strain ebn1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L9W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5L9W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetophenone_carboxylase Acetophenone carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.8 6.4.1.8] </span></td></tr> | | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetophenone_carboxylase Acetophenone carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.8 6.4.1.8] </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=5l9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l9w OCA], [http://pdbe.org/5l9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l9w RCSB], [http://www.ebi.ac.uk/pdbsum/5l9w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l9w ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5l9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l9w OCA], [http://pdbe.org/5l9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l9w RCSB], [http://www.ebi.ac.uk/pdbsum/5l9w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l9w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Acetophenone carboxylase]] | | [[Category: Acetophenone carboxylase]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Ermler, U]] | | [[Category: Ermler, U]] |
| | [[Category: Warkentin, E]] | | [[Category: Warkentin, E]] |
| | [[Category: Weidenweber, S]] | | [[Category: Weidenweber, S]] |
| | [[Category: Ligase]] | | [[Category: Ligase]] |
| Structural highlights
Function
[APCB_AROAE] Catalyzes the carboxylation of acetophenone to form 3-oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic catabolism of ethylbenzene. Also carboxylates propiophenone at the same rate and 4-acetyl-pyridine at lower rates.[1] [APCD_AROAE] Catalyzes the carboxylation of acetophenone to form 3-oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic catabolism of ethylbenzene. Also carboxylates propiophenone at the same rate and 4-acetyl-pyridine at lower rates.[2] [APCA_AROAE] Catalyzes the carboxylation of acetophenone to form 3-oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic catabolism of ethylbenzene. Also carboxylates propiophenone at the same rate and 4-acetyl-pyridine at lower rates.[3] [APCC_AROAE] Catalyzes the carboxylation of acetophenone to form 3-oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic catabolism of ethylbenzene. Also carboxylates propiophenone at the same rate and 4-acetyl-pyridine at lower rates.[4]
Publication Abstract from PubMed
Degradation of the aromatic ketone acetophenone is initiated by its carboxylation to benzoylacetate catalyzed by acetophenone carboxylase (Apc) in a reaction dependent on the hydrolysis of two ATP to ADP and Pi. Apc is a large protein complex which dissociates during purification into a heterooctameric Apc(alphaalpha'betagamma)2 core complex of 482 kDa and Apcepsilon of 34 kDa. In this report, we present the X-ray structure of the Apc(alphaalpha'betagamma)2 core complex from Aromatoleum aromaticum at ca. 3 A resolution which reveals a unique modular architecture and serves as model of a new enzyme family. Apcbeta contains a novel domain fold composed of two beta-sheets in a barrel-like arrangement running into a bundle of eight short polyproline (type II)-like helical segments. Apcalpha and Apcalpha' possess ATP binding modules of the ASKHA superfamily integrated into their multidomain structures and presumably operate as ATP-dependent kinases for acetophenone and bicarbonate, respectively. Mechanistic aspects of the novel carboxylation reaction requiring massive structural rearrangements are discussed and criteria for specifically annotating the family members Apc, acetone carboxylase and hydantoinase are defined.
Structure of the acetophenone carboxylase core complex: prototype of a new class of ATP-dependent carboxylases/hydrolases.,Weidenweber S, Schuhle K, Demmer U, Warkentin E, Ermler U, Heider J Sci Rep. 2017 Jan 5;7:39674. doi: 10.1038/srep39674. PMID:28054554[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jobst B, Schuhle K, Linne U, Heider J. ATP-dependent carboxylation of acetophenone by a novel type of carboxylase. J Bacteriol. 2010 Mar;192(5):1387-94. doi: 10.1128/JB.01423-09. Epub 2010 Jan 4. PMID:20047908 doi:http://dx.doi.org/10.1128/JB.01423-09
- ↑ Jobst B, Schuhle K, Linne U, Heider J. ATP-dependent carboxylation of acetophenone by a novel type of carboxylase. J Bacteriol. 2010 Mar;192(5):1387-94. doi: 10.1128/JB.01423-09. Epub 2010 Jan 4. PMID:20047908 doi:http://dx.doi.org/10.1128/JB.01423-09
- ↑ Jobst B, Schuhle K, Linne U, Heider J. ATP-dependent carboxylation of acetophenone by a novel type of carboxylase. J Bacteriol. 2010 Mar;192(5):1387-94. doi: 10.1128/JB.01423-09. Epub 2010 Jan 4. PMID:20047908 doi:http://dx.doi.org/10.1128/JB.01423-09
- ↑ Jobst B, Schuhle K, Linne U, Heider J. ATP-dependent carboxylation of acetophenone by a novel type of carboxylase. J Bacteriol. 2010 Mar;192(5):1387-94. doi: 10.1128/JB.01423-09. Epub 2010 Jan 4. PMID:20047908 doi:http://dx.doi.org/10.1128/JB.01423-09
- ↑ Weidenweber S, Schuhle K, Demmer U, Warkentin E, Ermler U, Heider J. Structure of the acetophenone carboxylase core complex: prototype of a new class of ATP-dependent carboxylases/hydrolases. Sci Rep. 2017 Jan 5;7:39674. doi: 10.1038/srep39674. PMID:28054554 doi:http://dx.doi.org/10.1038/srep39674
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