Sandbox ggc16: Difference between revisions
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==2PQ8 | ==(2PQ8) '''MYST Histone Acetyltransferase'''== | ||
<StructureSection load=' | <StructureSection load='2pq8' size='340' side='right' caption='Myst Histone Acetyltransferase' scene=''> | ||
MYST Histone Acetyltransferases (HAT), a diverse family of proteins responsible for a variety of functions in eukaryotes from yeast to humans<ref>PMID:11134336</ref>. These particular histone acetyltransferases are part of the MYST family because of their structure which includes <scene name='78/782639/Coenzyme_a/1'>coenzyme A</scene> and <scene name='78/782639/Zinc_ion/1'>Zinc Ion</scene>. | |||
== Function == | == Function == | ||
Highly conserved in eukaryotes, their key roles in post-translation modification of histones. Profound effect on chromatin structure in eukaryotes. Composed of an Acetyl-CoA binding motif and a zinc finger. The enzyme looks for lysine residues which are the universal target for acetylation, and by the addition of an acetyl group stablilizes the electrons of a histone making them less positively charged. | |||
== Relevance == | |||
These enzymes acetylate lysine amino acids of histone by transferring the acetyl group of acetyl CoA to form N-acetyllysine. While the DNA coiled around histones and the activity of histone acetyltransferase is able to turn genes on or off, along with influencing gene expression by acetylating non-histone proteins<ref>PMID:10441070</ref>. | |||
== Disease == | == Disease == | ||
HATs activate the residues of p53 by acetylation which leads to the elevation of p53 DNA binding or loss of its transcriptional activity<ref>PMID:10441070</ref>. If there’s any type of mutation where acetylation occurs of the p53 residues the functionality is hindered leading to the growth of tumors/cancers. | |||
== Structural highlights == | == Structural highlights == | ||
The binding site for this structure <scene name='78/782639/Coenzyme_a/3'>coenzyme A</scene>, which is involved in the transfer of an acetyl group from acetyl-CoA to the amine group of a lysine residue. The <scene name='78/782639/Zinc_ion/1'>zinc</scene> finger region of this structure is involved in the acetyltransferase activity and chromatin binding of the histone. The <scene name='78/782639/Cysteine_rich_structure/1'>cysteine</scene> residues are needed for catalyzing specific acetylation. | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
<ref>PMID:11134336</ref> | |||
<ref><ref>DOI: 10.1021/acschembio.5b00841</ref>PMID:11057899</ref> | |||