User:Jordan Finch/Sandbox 1

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==Histone Acetyltransferase HAT1/HAT2 Complex, ''Saccharomyces cerevisiae''==
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==Your Heading Here Histone Acetyltransferase Hat1/Hat2 Complex==
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<StructureSection load='4psw' size='350' frame='true' side='right' caption='HAT1 4PSW'
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<StructureSection load='4psw' size='340' side='right' caption='Hat1/Hat2 Complex' scene='4psw_overview'>
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This is a default text for your page '''Jordan Finch/Sandbox 2'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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This is a default text for your page '''Caitlin Marie Gaich/Sandbox1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Introduction ==
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== Function ==
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[https://en.wikipedia.org/wiki/Histone Histone background]
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== HAT1 Background ==
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[[Image:Main_bonding_cartoon_3.png|400px|right|thumb|Figure 1]]
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== Hat1/Hat2 Complex Structure ==
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Hat1 is not catalytically active until it binds with HAT2 to form the <scene name='81/811718/Hat1_hat2_complex_aco_and_h4/1'>complex</scene>. HAT1 structure includes 317 residues and is identified as <scene name='81/811718/Hat1_protein/1'>chain A</scene>. HAT2 is identified as <scene name='81/811718/Hat2_protein/1'>chain B</scene>, which includes 401 residues. The activated complex acetylates residues in the 38 residue span of <scene name='81/811718/Portion_of_histone_4/1'>Histone 4</scene>.
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== Disease ==
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== Mechanism ==
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== Relevance ==
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Of the five classes of HAT enzymes, the catalytic mechanisms for two of those enzymes, HAT1 and Rtt109, remains unclear. A structural overlay of HAT1 and Gcn5, a more well-known and understood HAT enzyme, found a conserved glutamate residue in the active site of both molecules. It was found that mutation at that active site glutamate residue greatly alters the catalytic ability of HAT1 and has been proven to be structurally important. <ref> DOI:10.1101/gad.240531.114 </ref> Using this information and structural information regarding the proximity of potentially catalytic residues, the most plausible mechanism for histone acetylation involves the following relevant residues and cofactors <scene name='81/811713/Mechanism_glu_lys_coa/1'>Glu255, Lys14, and AcetylCoA</scene>.
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In this mechanism, the glutamate at residue 255 acts as a general base and deprotonates lysine 12 of histone 4 (the numbering of the modified lysine residue on histone 4 is shifted two residues).The deprotonated lysine then acts as a nucleophile and attacks the carbonyl carbon of acetyl coenzyme A (CoA, forming a tetrahedral intermediate transition state. The negative charge on the oxygen collapses down to for a double bond and the scissle bond between the carbonyl carbon and the sulfur atom of acetyl CoA is broken. The resulting product of this reaction is histone 4 with an acetyl-lysine at residue 12 and CoEnzyme A.
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== Structural highlights ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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== Application ==
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</StructureSection>
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== References ==
== References ==
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Li, Y. et. al. ''Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.''(2014). ''Genes Dev.''28:1217-1227. DOI:10.1101/gad.240531.114
 
<references/>
<references/>
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== Student Contributors ==
 
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* Caitlin Gaich
 
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* Jordan Finch
 
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* Morgan Buckley
 

Revision as of 18:28, 5 April 2019

Your Heading Here Histone Acetyltransferase Hat1/Hat2 Complex

Hat1/Hat2 Complex

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Jordan Finch

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