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4HDK

Crystal Structure of ArsAB in Complex with Phloroglucinol

Summary for 4HDK
Entry DOI10.2210/pdb4hdk/pdb
Related4HDM 4HDN 4HDR 4HDS
DescriptorArsA, ArsB, CHLORIDE ION, ... (6 entities in total)
Functional Keywordstransferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological sourceSporomusa ovata
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Total number of polymer chains2
Total formula weight73015.73
Authors
Newmister, S.A.,Chan, C.H.,Escalante-Semerena, J.C.,Rayment, I. (deposition date: 2012-10-02, release date: 2012-10-24, Last modification date: 2024-02-28)
Primary citationNewmister, S.A.,Chan, C.H.,Escalante-Semerena, J.C.,Rayment, I.
Structural Insights into the Function of the Nicotinate Mononucleotide:phenol/p-cresol Phosphoribosyltransferase (ArsAB) Enzyme from Sporomusa ovata.
Biochemistry, 51:8571-8582, 2012
Cited by
PubMed Abstract: Cobamides (Cbas) are cobalt (Co) containing tetrapyrrole-derivatives involved in enzyme-catalyzed carbon skeleton rearrangements, methyl-group transfers, and reductive dehalogenation. The biosynthesis of cobamides is complex and is only performed by some bacteria and achaea. Cobamides have an upper (Coβ) ligand (5'-deoxyadenosyl or methyl) and a lower (Coα) ligand base that contribute to the axial Co coordinations. The identity of the lower Coα ligand varies depending on the organism synthesizing the Cbas. The homoacetogenic bacterium Sporomusa ovata synthesizes two unique phenolic cobamides (i.e., Coα-(phenolyl/p-cresolyl)cobamide), which are used in the catabolism of methanol and 3,4-dimethoxybenzoate by this bacterium. The S. ovata ArsAB enzyme activates a phenolic lower ligand prior to its incorporation into the cobamide. ArsAB consists of two subunits, both of which are homologous (∼35% identity) to the well-characterized Salmonella enterica CobT enzyme, which transfers nitrogenous bases such as 5,6-dimethylbenzimidazole (DMB) and adenine, but cannot utilize phenolics. Here we report the three-dimensional structure of ArsAB, which shows that the enzyme forms a pseudosymmetric heterodimer, provide evidence that only the ArsA subunit has base:phosphoribosyl-transferase activity, and propose a mechanism by which phenolic transfer is facilitated by an activated water molecule.
PubMed: 23039029
DOI: 10.1021/bi301142h
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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数据于2024-11-06公开中

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