4QLO
Crystal Structure of homoserine o-acetyltransferase from Staphylococcus aureus
Summary for 4QLO
| Entry DOI | 10.2210/pdb4qlo/pdb |
| Descriptor | homoserine O-acetyltransferase (2 entities in total) |
| Functional Keywords | rossmann fold, acetyltransferase, acetylco-a binding, transferase |
| Biological source | Staphylococcus aureus subsp. aureus |
| Cellular location | Cytoplasm (By similarity): A8YYT5 |
| Total number of polymer chains | 1 |
| Total formula weight | 41244.43 |
| Authors | Thangavelu, B.,Pavlovsky, A.G.,Viola, R.E. (deposition date: 2014-06-12, release date: 2014-08-20, Last modification date: 2024-02-28) |
| Primary citation | Thangavelu, B.,Pavlovsky, A.G.,Viola, R. Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure. Acta Crystallogr.,Sect.F, 70:1340-1345, 2014 Cited by PubMed Abstract: Homoserine O-acetyltransferase (HTA) catalyzes the formation of L-O-acetyl-homoserine from L-homoserine through the transfer of an acetyl group from acetyl-CoA. This is the first committed step required for the biosynthesis of methionine in many fungi, Gram-positive bacteria and some Gram-negative bacteria. The structure of HTA from Staphylococcus aureus (SaHTA) has been determined to a resolution of 2.45 Å. The structure belongs to the α/β-hydrolase superfamily, consisting of two distinct domains: a core α/β-domain containing the catalytic site and a lid domain assembled into a helical bundle. The active site consists of a classical catalytic triad located at the end of a deep tunnel. Structure analysis revealed some important differences for SaHTA compared with the few known structures of HTA. PubMed: 25286936DOI: 10.1107/S2053230X14018664 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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