3Q9B
Crystal Structure of APAH complexed with M344
Summary for 3Q9B
| Entry DOI | 10.2210/pdb3q9b/pdb |
| Related | 3Q9C 3Q9E 3Q9F |
| Descriptor | Acetylpolyamine amidohydrolase, DIMETHYL SULFOXIDE, 4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide, ... (7 entities in total) |
| Functional Keywords | hdac, polyamines, arginase fold, deacetylase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Mycoplana ramosa (Mycoplana bullata) |
| Total number of polymer chains | 12 |
| Total formula weight | 450526.97 |
| Authors | Lombardi, P.M.,Christianson, D.W. (deposition date: 2011-01-07, release date: 2011-03-02, Last modification date: 2023-09-13) |
| Primary citation | Lombardi, P.M.,Angell, H.D.,Whittington, D.A.,Flynn, E.F.,Rajashankar, K.R.,Christianson, D.W. Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases . Biochemistry, 50:1808-1817, 2011 Cited by PubMed Abstract: Polyamines are a ubiquitous class of polycationic small molecules that can influence gene expression by binding to nucleic acids. Reversible polyamine acetylation regulates nucleic acid binding and is required for normal cell cycle progression and proliferation. Here, we report the structures of Mycoplana ramosa acetylpolyamine amidohydrolase (APAH) complexed with a transition state analogue and a hydroxamate inhibitor and an inactive mutant complexed with two acetylpolyamine substrates. The structure of APAH is the first of a histone deacetylase-like oligomer and reveals that an 18-residue insert in the L2 loop promotes dimerization and the formation of an 18 Å long "L"-shaped active site tunnel at the dimer interface, accessible only to narrow and flexible substrates. The importance of dimerization for polyamine deacetylase function leads to the suggestion that a comparable dimeric or double-domain histone deacetylase could catalyze polyamine deacetylation reactions in eukaryotes. PubMed: 21268586DOI: 10.1021/bi101859k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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