Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5M45

Structure of Acetone Carboxylase purified from Xanthobacter autotrophicus

Summary for 5M45
Entry DOI10.2210/pdb5m45/pdb
DescriptorAcetone carboxylase alpha subunit, Acetone carboxylase beta subunit, Acetone carboxylase gamma subunit, ... (10 entities in total)
Functional Keywordscarboxylation, ligase
Biological sourceXanthobacter autotrophicus Py2
More
Total number of polymer chains12
Total formula weight744035.30
Authors
Kabasakal, B.V.,Wells, J.N.,Nwaobi, B.C.,Eilers, B.J.,Peters, J.W.,Murray, J.W. (deposition date: 2016-10-18, release date: 2017-08-09, Last modification date: 2024-01-17)
Primary citationMus, F.,Eilers, B.J.,Alleman, A.B.,Kabasakal, B.V.,Wells, J.N.,Murray, J.W.,Nocek, B.P.,DuBois, J.L.,Peters, J.W.
Structural Basis for the Mechanism of ATP-Dependent Acetone Carboxylation.
Sci Rep, 7:7234-7234, 2017
Cited by
PubMed Abstract: Microorganisms use carboxylase enzymes to form new carbon-carbon bonds by introducing carbon dioxide gas (CO) or its hydrated form, bicarbonate (HCO), into target molecules. Acetone carboxylases (ACs) catalyze the conversion of substrates acetone and HCO 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 (αβγ) 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 CO into biomass, a process of great significance to the global carbon cycle.
PubMed: 28775283
DOI: 10.1038/s41598-017-06973-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.87 Å)
Structure validation

227561

건을2024-11-20부터공개중

PDB statisticsPDBj update infoContact PDBjnumon