|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='5svb' size='340' side='right'caption='[[5svb]], [[Resolution|resolution]] 2.65Å' scene=''> | | <StructureSection load='5svb' size='340' side='right'caption='[[5svb]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5svb]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanp2 Xanp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SVB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SVB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5svb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthobacter_autotrophicus_Py2 Xanthobacter autotrophicus Py2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SVB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.645Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acxB, Xaut_3510 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=78245 XANP2]), acxA, Xaut_3509 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=78245 XANP2]), acxC, Xaut_3511 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=78245 XANP2])</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=5svb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5svb OCA], [https://pdbe.org/5svb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5svb RCSB], [https://www.ebi.ac.uk/pdbsum/5svb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5svb ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetone_carboxylase Acetone carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.6 6.4.1.6] </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=5svb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5svb OCA], [http://pdbe.org/5svb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5svb RCSB], [http://www.ebi.ac.uk/pdbsum/5svb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5svb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACXB_XANP2 ACXB_XANP2]] Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.<ref>PMID:9237998</ref> [[http://www.uniprot.org/uniprot/ACXC_XANP2 ACXC_XANP2]] Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.<ref>PMID:9237998</ref> [[http://www.uniprot.org/uniprot/ACXA_XANP2 ACXA_XANP2]] Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.<ref>PMID:9237998</ref> | + | [https://www.uniprot.org/uniprot/ACXB_XANP2 ACXB_XANP2] Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.<ref>PMID:9237998</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acetone carboxylase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xanp2]] | + | [[Category: Xanthobacter autotrophicus Py2]] |
| - | [[Category: Alleman, A B]] | + | [[Category: Alleman AB]] |
| - | [[Category: Dubois, J L]] | + | [[Category: Dubois JL]] |
| - | [[Category: Eilers, B J]] | + | [[Category: Eilers BJ]] |
| - | [[Category: Kabasakal, B V]] | + | [[Category: Kabasakal BV]] |
| - | [[Category: Murray, J W]] | + | [[Category: Murray JW]] |
| - | [[Category: Mus, F]] | + | [[Category: Mus F]] |
| - | [[Category: Nocek, B P]] | + | [[Category: Nocek BP]] |
| - | [[Category: Peters, J W]] | + | [[Category: Peters JW]] |
| - | [[Category: Acetoacetate]]
| + | |
| - | [[Category: Amp]]
| + | |
| - | [[Category: Atp]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Manganese]]
| + | |
| - | [[Category: Zinc]]
| + | |
| Structural highlights
5svb is a 6 chain structure with sequence from Xanthobacter autotrophicus Py2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.645Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
ACXB_XANP2 Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.[1]
Publication Abstract from PubMed
Microorganisms use carboxylase enzymes to form new carbon-carbon bonds by introducing carbon dioxide gas (CO2) or its hydrated form, bicarbonate (HCO3-), into target molecules. Acetone carboxylases (ACs) catalyze the conversion of substrates acetone and HCO3- to form the product acetoacetate. Many bicarbonate-incorporating carboxylases rely on the organic cofactor biotin for the activation of bicarbonate. ACs contain metal ions but not organic cofactors, and use ATP to activate substrates through phosphorylation. How the enzyme coordinates these phosphorylation events and new C-C bond formation in the absence of biotin has remained a mystery since these enzymes were discovered. The first structural rationale for acetone carboxylation is presented here, focusing on the 360 kDa (alphabetagamma)2 heterohexameric AC from Xanthobacter autotrophicus in the ligand-free, AMP-bound, and acetate coordinated states. These structures suggest successive steps in a catalytic cycle revealing that AC undergoes large conformational changes coupled to substrate activation by ATP to perform C-C bond ligation at a distant Mn center. These results illustrate a new chemical strategy for the conversion of CO2 into biomass, a process of great significance to the global carbon cycle.
Structural Basis for the Mechanism of ATP-Dependent Acetone Carboxylation.,Mus F, Eilers BJ, Alleman AB, Kabasakal BV, Wells JN, Murray JW, Nocek BP, DuBois JL, Peters JW Sci Rep. 2017 Aug 3;7(1):7234. doi: 10.1038/s41598-017-06973-8. PMID:28775283[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sluis MK, Ensign SA. Purification and characterization of acetone carboxylase from Xanthobacter strain Py2. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8456-61. PMID:9237998
- ↑ Mus F, Eilers BJ, Alleman AB, Kabasakal BV, Wells JN, Murray JW, Nocek BP, DuBois JL, Peters JW. Structural Basis for the Mechanism of ATP-Dependent Acetone Carboxylation. Sci Rep. 2017 Aug 3;7(1):7234. doi: 10.1038/s41598-017-06973-8. PMID:28775283 doi:http://dx.doi.org/10.1038/s41598-017-06973-8
|
