5C88
Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form
Summary for 5C88
Entry DOI | 10.2210/pdb5c88/pdb |
Descriptor | Uncharacterized N-acetyltransferase SSO0209, COENZYME A (3 entities in total) |
Functional Keywords | acetyltransferase, transferase |
Biological source | Sulfolobus solfataricus strain P2 |
Cellular location | Cytoplasm : Q980R9 |
Total number of polymer chains | 2 |
Total formula weight | 42139.95 |
Authors | Chang, Y.Y.,Hsu, C.H. (deposition date: 2015-06-25, release date: 2016-01-13, Last modification date: 2023-11-08) |
Primary citation | Chang, Y.Y.,Hsu, C.H. Multiple Conformations of the Loop Region Confers Heat-Resistance on SsArd1, a Thermophilic NatA. Chembiochem, 17:214-217, 2016 Cited by PubMed Abstract: Structural comparison indicates that the loop region between β3 and β4 of SsArd1 is extended relative to the corresponding region in mesophilic Nats, and forms a plastic hydrogen-bond network mainly at two serine residues. Strikingly, two single-point mutants showed ∼3 °C decrease in melting temperature, and two other variants showed ∼7 °C decrease; this correlated with significantly reduced enzymatic activity. To our knowledge, this is the first discovery of a loop region capable of remarkably improving protein thermostability. This provides a novel route to engineer heat-resistant proteins. PubMed: 26593285DOI: 10.1002/cbic.201500568 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
Download full validation report