DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol [1] to the rescue.
Introduction
Histone background
HAT1 Background
Hat1/Hat2 Complex Structure
Hat1 is not catalytically active until it binds with HAT2 to form the . HAT1 structure includes 317 residues and is identified as . HAT2 is identified as , which includes 401 residues. The activated complex acetylates residues in the 38 residue span of .
The HAT1 and HAT2 interface is stabilized by hydrogen bonds, , and hydrophobic interactions. Most of these interactions are located in of the HAT1 domain, which forms a well-ordered helix. This LP1 helix is thought to be important for the heterodimer formation as the deletion of LP1 abolished the interaction between HAT1 and HAT2. This suggests that there may be another protein involved such as the N terminus tail of H4 acting as a linker protein interacting with the complex interface. The three major areas where hydrogen bonds are present aids in this complex formation. The side chain atoms of with the main chain nitrogen of Ala202 in HAT1. The side chain of makes hydrogen bonds with Leu288 and Phe205 respectively. The last area of hydrogen bonds between HAT1 and HAT is found between . The at the interface of the complex appears to be critical for the complex formation. This core consists of aromatic amino acids from HAT1 and leucine amino acids from HAT2, however it does not form any obvious ring stacking.
Mechanism
Application
References
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
- ↑ 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
Student Contributors
- Caitlin Gaich
- Jordan Finch
- Morgan Buckley
