Sandbox Reserved 774: Difference between revisions

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=Introduction=
=Introduction=


My protein is Histone Acetyltransferase HPA2. HPA2 is a member of the GNAT (Gcn5-related N-acetyltransferases) super-family of enzymes that are found spread out across nature and use acyl-CoA's to acylate their cognate substrates. Histone Acetyltransferase HPA2 is found in the organism Saccharomyces Cerevisiae, which is more commonly known as Baker's Yeast. In vitro, HPA2 serves to acetylate histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12.' In solution, HPA2 forms a dimer, and upon binding with AcCoA forms a tetramer. It is a transferase class protein.
My protein is Histone Acetyltransferase Hpa2. Hpa2 is a member of the GNAT (Gcn5-related N-acetyltransferases) super-family of enzymes that are found spread out across nature and use acyl-CoA's to acylate their cognate substrates. Histone Acetyltransferase Hpa2 is found in the organism Saccharomyces Cerevisiae, which is more commonly known as Baker's Yeast. In vitro, Hpa2 serves to acetylate histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12.' In solution, Hpa2 forms a dimer, and upon binding with AcCoA forms a tetramer. It is classified as a transferase.


=Structure=
=Structure=
Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA). The method used to determine the structure was X-ray crystallography. Crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The average B-factor value is 23.9 (main chain) with a 25.4 side chain. The R-factor is 0.19.


==Description==
==Description==