3f8k

Crystal structure of protein acetyltransferase (PAT) from Sulfolobus solfataricus

spinqualitylabelsall models 3f8k, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3f8k is a 1 chain structure with sequence from Saccharolobus solfataricus P2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.84Å Ligands: COA, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAT_SACS2 Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Sulfolobus solfataricus protein acetyltransferase (PAT) acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys(16) to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a "primitive" model for chromatin regulation analogous to histone modification in eukaryotes. We report the 1.84-A crystal structure of PAT in complex with coenzyme A. The structure reveals homology to both prokaryotic GNAT acetyltransferases and eukaryotic histone acetyltransferases (HATs), with an additional "bent helix" proximal to the substrate binding site that might play an autoregulatory function. Investigation of active site mutants suggests that PAT does not use a single general base or acid residue for substrate deprotonation and product reprotonation, respectively, and that a diffusional step, such as substrate binding, may be rate-limiting. The catalytic efficiency of PAT toward ALBA is low relative to other acetyltransferases, suggesting that there may be better, unidentified substrates for PAT. The structural similarity of PAT to eukaryotic HATs combined with its conserved role in chromatin regulation suggests that PAT is evolutionarily related to the eukaryotic HATs. Structure and biochemical characterization of protein acetyltransferase from Sulfolobus solfataricus.,Brent MM, Iwata A, Carten J, Zhao K, Marmorstein R J Biol Chem. 2009 Jul 17;284(29):19412-9. Epub 2009 May 27. PMID:19473964 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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