User:Caitlin Marie Gaich/Sandbox1
From Proteopedia
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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>. | 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>. | ||
| - | The HAT1 and HAT2 interface is stabilized by hydrogen bonds, salt bridges, and hydrophobic interactions. Most of these interactions are located in LP1 of the HAT1 domain, which forms a well-ordered helix. There are three major areas where hydrogen bonds are present. The side chain atoms of <scene name='81/811717/Lys211phe205_and_leu288arg282/ | + | The HAT1 and HAT2 interface is stabilized by hydrogen bonds, salt bridges, and hydrophobic interactions. Most of these interactions are located in LP1 of the HAT1 domain, which forms a well-ordered helix. There are three major areas where hydrogen bonds are present. The side chain atoms of <scene name='81/811717/Lys211phe205_and_leu288arg282/6'>Tyr199 and Asp308</scene> with the main chain nitrogen of Ala202 in HAT1. The side chain of <scene name='81/811717/Lys211phe205_and_leu288arg282/4'>Lys211 and Arg282</scene> makes hydrogen bonds with Leu288 and Phe205 respectively. The last area of hydrogen bonds between HAT1 and HAT is found between <scene name='81/811717/Serine_hydrogen_bonds/3'>Ser263 and Asp 206</scene>. |
Revision as of 02:32, 11 April 2019
Histone Acetyltransferase HAT1/HAT2 Complex, Saccharomyces cerevisiae
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