1BOB
HISTONE ACETYLTRANSFERASE HAT1 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A
Summary for 1BOB
| Entry DOI | 10.2210/pdb1bob/pdb |
| Descriptor | HISTONE ACETYLTRANSFERASE, CALCIUM ION, ACETYL COENZYME *A, ... (4 entities in total) |
| Functional Keywords | histone acetyltransferase, histone modification, acetyl coenzyme a binding-protein, acetyltransferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 38415.99 |
| Authors | Dutnall, R.N.,Tafrov, S.T.,Sternglanz, R.,Ramakrishnan, V. (deposition date: 1998-07-02, release date: 1999-04-20, Last modification date: 2024-02-07) |
| Primary citation | Dutnall, R.N.,Tafrov, S.T.,Sternglanz, R.,Ramakrishnan, V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell(Cambridge,Mass.), 94:427-438, 1998 Cited by PubMed Abstract: We have solved the crystal structure of the yeast histone acetyltransferase Hat1-acetyl coenzyme A (AcCoA) complex at 2.3 A resolution. Hat1 has an elongated, curved structure, and the AcCoA molecule is bound in a cleft on the concave surface of the protein, marking the active site of the enzyme. A channel of variable width and depth that runs across the protein is probably the binding site for the histone substrate. A model for histone H4 binding by Hat1 is discussed in terms of possible sources of specific lysine recognition by the enzyme. The structure of Hat1 provides a model for the structures of the catalytic domains of a protein superfamily that includes other histone acetyltransferases such as Gcn5 and CBP. PubMed: 9727486DOI: 10.1016/S0092-8674(00)81584-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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