3q9b

Crystal Structure of APAH complexed with M344

spinqualitylabelsall models 3q9b, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q9b is a 12 chain structure with sequence from Atcc 49678. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: B3N, DMS, K, NA, ZN Related: 3q9c, 3q9e, 3q9f Gene: aphA, aph (ATCC 49678) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [APHA_MYCRA] Acts on many types of acetylpolyamines. Has high affinity towards acetylputrescine, acetylcadaverine, acetylspermidine, and acetylspermine. Acts on L-Lys-(epsilon-acetyl)-coumarin, but has very low activity towards acetylated peptides. Publication Abstract from PubMed 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 A 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. Structure of Prokaryotic Polyamine Deacetylase Reveals Evolutionary Functional Relationships with Eukaryotic Histone Deacetylases .,Lombardi PM, Angell HD, Whittington DA, Flynn EF, Rajashankar KR, Christianson DW Biochemistry. 2011 Jan 26. PMID:21268586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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