3Q1P
Crystal structure of CDP-Chase
Summary for 3Q1P
| Entry DOI | 10.2210/pdb3q1p/pdb |
| Related | 3Q4I |
| Descriptor | Phosphohydrolase (MutT/nudix family protein), SULFATE ION (3 entities in total) |
| Functional Keywords | nudix, asymmetric dimer, hydrolase, rna exonuclease, cdp-choline pyrophosphatase |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 2 |
| Total formula weight | 48098.83 |
| Authors | Duong-Ly, K.C.,Gabelli, S.B.,Amzel, L.M. (deposition date: 2010-12-17, release date: 2011-07-13, Last modification date: 2024-11-06) |
| Primary citation | Duong-Ly, K.C.,Gabelli, S.B.,Xu, W.,Dunn, C.A.,Schoeffield, A.J.,Bessman, M.J.,Amzel, L.M. The Nudix Hydrolase CDP-Chase, a CDP-Choline Pyrophosphatase, Is an Asymmetric Dimer with Two Distinct Enzymatic Activities. J.Bacteriol., 193:3175-3185, 2011 Cited by PubMed Abstract: A Nudix enzyme from Bacillus cereus (NCBI RefSeq accession no. NP_831800) catalyzes the hydrolysis of CDP-choline to produce CMP and phosphocholine. Here, we show that in addition, the enzyme has a 3'→5' RNA exonuclease activity. The structure of the free enzyme, determined to a 1.8-Å resolution, shows that the enzyme is an asymmetric dimer. Each monomer consists of two domains, an N-terminal helical domain and a C-terminal Nudix domain. The N-terminal domain is placed relative to the C-terminal domain such as to result in an overall asymmetric arrangement with two distinct catalytic sites: one with an "enclosed" Nudix pyrophosphatase site and the other with a more open, less-defined cavity. Residues that may be important for determining the asymmetry are conserved among a group of uncharacterized Nudix enzymes from Gram-positive bacteria. Our data support a model where CDP-choline hydrolysis is catalyzed by the enclosed Nudix site and RNA exonuclease activity is catalyzed by the open site. CDP-Chase is the first identified member of a novel Nudix family in which structural asymmetry has a profound effect on the recognition of substrates. PubMed: 21531795DOI: 10.1128/JB.00089-11 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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