Sandbox ggc16: Difference between revisions
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== | ==(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 == | ||
<scene name='78/782639/ | 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> | |||
Latest revision as of 18:32, 20 November 2019
(2PQ8) MYST Histone Acetyltransferase(2PQ8) MYST Histone Acetyltransferase
MYST Histone Acetyltransferases (HAT), a diverse family of proteins responsible for a variety of functions in eukaryotes from yeast to humans[1]. These particular histone acetyltransferases are part of the MYST family because of their structure which includes and . FunctionHighly 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. RelevanceThese 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[2]. DiseaseHATs activate the residues of p53 by acetylation which leads to the elevation of p53 DNA binding or loss of its transcriptional activity[3]. 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 highlightsThe binding site for this structure , which is involved in the transfer of an acetyl group from acetyl-CoA to the amine group of a lysine residue. The finger region of this structure is involved in the acetyltransferase activity and chromatin binding of the histone. The residues are needed for catalyzing specific acetylation.
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ReferencesReferences
- ↑ Chen CJ, Deng Z, Kim AY, Blobel GA, Lieberman PM. Stimulation of CREB binding protein nucleosomal histone acetyltransferase activity by a class of transcriptional activators. Mol Cell Biol. 2001 Jan;21(2):476-87. doi: 10.1128/MCB.21.2.476-487.2001. PMID:11134336 doi:http://dx.doi.org/10.1128/MCB.21.2.476-487.2001
- ↑ Grant PA, Berger SL. Histone acetyltransferase complexes. Semin Cell Dev Biol. 1999 Apr;10(2):169-77. doi: 10.1006/scdb.1999.0298. PMID:10441070 doi:http://dx.doi.org/10.1006/scdb.1999.0298
- ↑ Grant PA, Berger SL. Histone acetyltransferase complexes. Semin Cell Dev Biol. 1999 Apr;10(2):169-77. doi: 10.1006/scdb.1999.0298. PMID:10441070 doi:http://dx.doi.org/10.1006/scdb.1999.0298
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Cite error: Closing </ref> missing for <ref> tagPMID:11057899</ref>