Sandbox Reserved 774
From Proteopedia
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=Introduction= | =Introduction= | ||
| - | My protein is Histone Acetyltransferase | + | My protein is Histone Acetyltransferase Hpa2. Hpa2 is a member of the GNAT (Gcn5-related N-acetyltransferases) super-family of enzymes that are found spread out across nature and use acyl-CoA's to acylate their cognate substrates. Histone Acetyltransferase Hpa2 is found in the organism Saccharomyces Cerevisiae, which is more commonly known as Baker's Yeast. In vitro, Hpa2 serves to acetylate histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12.' In solution, Hpa2 forms a dimer, and upon binding with AcCoA forms a tetramer. It is classified as a transferase. |
=Structure= | =Structure= | ||
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| + | Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA). The method used to determine the structure was X-ray crystallography. Crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The average B-factor value is 23.9 (main chain) with a 25.4 side chain. The R-factor is 0.19. | ||
==Description== | ==Description== | ||
Revision as of 01:30, 27 November 2013
| This Sandbox is Reserved from Sep 25, 2013, through Mar 31, 2014 for use in the course "BCH455/555 Proteins and Molecular Mechanisms" taught by Michael B. Goshe at the North Carolina State University. This reservation includes Sandbox Reserved 299, Sandbox Reserved 300 and Sandbox Reserved 760 through Sandbox Reserved 779. |
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Contents |
Introduction
My protein is Histone Acetyltransferase Hpa2. Hpa2 is a member of the GNAT (Gcn5-related N-acetyltransferases) super-family of enzymes that are found spread out across nature and use acyl-CoA's to acylate their cognate substrates. Histone Acetyltransferase Hpa2 is found in the organism Saccharomyces Cerevisiae, which is more commonly known as Baker's Yeast. In vitro, Hpa2 serves to acetylate histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12.' In solution, Hpa2 forms a dimer, and upon binding with AcCoA forms a tetramer. It is classified as a transferase.
Structure
Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA). The method used to determine the structure was X-ray crystallography. Crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The average B-factor value is 23.9 (main chain) with a 25.4 side chain. The R-factor is 0.19.
Description
This structure contains ... alpha helices...
3D Structure
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Mechanism
Implications
The analysis of a loss-of-function mutant of the hpa2 gene suggests that the hpa2 affects bacterial proliferation in host plants and a hypersensitive response in nonhost plants. As this is the first of such enzyme activity identified in the Hrp protein family, we speculate that the Hpa2 contributes to the assembly of the TTSS by enlarging gaps in the peptidoglycan meshwork of bacterial cell walls
SHIVA
