5c88

Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form

spinqualitylabelsall models 5c88, resolution 2.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c88 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: COA Activity: Peptide alpha-N-acetyltransferase, with EC number 2.3.1.88 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed Structural comparison indicates the loop region between beta3 and beta4 of SsArd1 was more extended than corresponding region of mesophilic Nats and formed a plastically hydrogen bond network mainly via two Ser residues. Strikingly, two single-point mutants showed ~3 degrees C decrease in melting temperature, while two other variants showed a ~7 degrees C decrease in melting temperature, which correlated to the seriously reducing enzymatic activity. To our knowledge, this is the first discovery of a loop region capable of remarkably improving protein thermostability and to provide a novel possibility to engineer heat-resistant proteins. Multiple conformations of the loop region confers heat-resistance of SsArd1, a thermophilic NatA.,Chang YY, Hsu CH Chembiochem. 2015 Nov 23. doi: 10.1002/cbic.201500568. PMID:26593285 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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