Sandbox ggc16: Difference between revisions

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-==2PQ8 Structure '''Myst Histone Acetyltransferase'''==
+==(2PQ8)  '''MYST Histone Acetyltransferase'''==
 <StructureSection load='2pq8' size='340' side='right' caption='Myst Histone Acetyltransferase' scene=''>
-Part of the Myst Family, this histone modifier adds and removes a variety of chemical moieties to histone residues. Such modifications on a single or on several neighboring nucleosomes combine to produce a specific effect on the local chromatin structure.
+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>.
-You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI: 10.1021/acschembio.5b00841</ref> or to the article describing Jmol <ref>PMID:11134336</ref> to the rescue.<ref>PMID:10441070</ref>
 == 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.
+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 ==
-residues of p53 acetylated by HATs may be located in variable sites, which leads to elevation of p53 DNA binding or loss of its transcriptional activity. It has been demonstrated that mutation of the C-terminal site of p53, where acetylation occurs, prompts comprehensively the loss of p53-dependent cyclin-dependent kinase inhibitor p21 transcription [49,50]. Acetylation of signal mediators may be prominent in subsequent stages in cancer progression.
+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.
-== Relevance ==
 == Structural highlights ==
-<scene name='78/782639/Binding_mode_of_dc_m01/1'>DC_M01</scene>
+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.
-<scene name='78/782639/N_to_c_rainbow/2'>N to C Sequence</scene>
 </StructureSection>
 == References ==
 <references/>
+<ref>PMID:11134336</ref>
+<ref><ref>DOI: 10.1021/acschembio.5b00841</ref>PMID:11057899</ref>