Sandbox Reserved 774: Difference between revisions

Line 7:

=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<ref name=desperate>"Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae." Protein Data Bank. EMDataBank, n.d. Web. 17 Nov. 2013.[http://www.rcsb.org/pdb/explore/explore.do?structureId=1QSO RCSB.org]</ref>. 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<ref name=desperate/><ref name=Shiva/>. It is classified as a transferase.<ref name=Shiva>Angus-Hill, et al. "Crystal Structure of the Histone Acetyltransferase Hpa2: a Tetrameric Member of the Gcn5-related N-acetyltransferase Superfamily." J. Mol. Biol. 1999.3338 (1999): 1-14. Web. 18 Nov. 2013.</ref>

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.<ref name=desperate>"Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae." Protein Data Bank. EMDataBank, n.d. Web. 17 Nov. 2013.[http://www.rcsb.org/pdb/explore/explore.do?structureId=1QSO RCSB.org]</ref> Histone Acetyltransferase Hpa2 is found in the organism Saccharomyces Cerevisiae, which is more commonly known as Baker's Yeast.<ref>"Q06592 (HPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot." Unitprot.org. UniProtKB, 13 Nov. 2013. Web. 16 Nov. 2013.[http://www.uniprot.org/uniprot/Q06592 UnitPro.org]</ref> 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.<ref name=desperate/><ref name=Shiva/> It is classified as a transferase.<ref name=Shiva>Angus-Hill, et al. "Crystal Structure of the Histone Acetyltransferase Hpa2: a Tetrameric Member of the Gcn5-related N-acetyltransferase Superfamily." J. Mol. Biol. 1999.3338 (1999): 1-14. Web. 18 Nov. 2013.</ref>

=Structure=

Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA)<ref name=Shiva/>. The method used to determine the structure was [[X-ray crystallography]]. Sedimentation and crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The crystal structure of the oligomer reveals that two Hpa2 dimers are held together by interaction between the bound acetyl-CoA molecules. The average B-factor value is 23.9 (<scene name='56/564050/Bakhbone_mainechain/1'>main chain</scene>) with a 25.4 <scene name='56/564050/Sidechain/2'>side chain</scene>. The R-factor is 0.19 <ref name=Shiva/>. Core fold features include four conserved sequence motifs of the GNAT family and comprises a central highly curved five stranded <scene name='56/564050/Beta_sheets/1'>Beta sheets</scene> (β1-β5) surrounded on both sides by helical segments (α1 and α3)<ref name=Shiva/>.

Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA).<ref name=Shiva/> The method used to determine the structure was [[X-ray crystallography]]. Sedimentation and crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The crystal structure of the oligomer reveals that two Hpa2 dimers are held together by interaction between the bound acetyl-CoA molecules. The average B-factor value is 23.9 (<scene name='56/564050/Bakhbone_mainechain/1'>main chain</scene>) with a 25.4 <scene name='56/564050/Sidechain/2'>side chain</scene>. The R-factor is 0.19. <ref name=Shiva/> Core fold features include four conserved sequence motifs of the GNAT family and comprises a central highly curved five stranded <scene name='56/564050/Beta_sheets/1'>Beta sheets</scene> (β1-β5) surrounded on both sides by helical segments (α1 and α3).<ref name=Shiva/>

=Secondary Structure=

Sandbox Reserved 774: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 7: / Line 7: @@
 =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<ref name=desperate>"Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae." Protein Data Bank. EMDataBank, n.d. Web. 17 Nov. 2013.[http://www.rcsb.org/pdb/explore/explore.do?structureId=1QSO RCSB.org]</ref>. 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<ref name=desperate/><ref name=Shiva/>. It is classified as a transferase.<ref name=Shiva>Angus-Hill, et al. "Crystal Structure of the Histone Acetyltransferase Hpa2: a Tetrameric Member of the Gcn5-related N-acetyltransferase Superfamily." J. Mol. Biol. 1999.3338 (1999): 1-14. Web. 18 Nov. 2013.</ref>
+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.<ref name=desperate>"Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae." Protein Data Bank. EMDataBank, n.d. Web. 17 Nov. 2013.[http://www.rcsb.org/pdb/explore/explore.do?structureId=1QSO RCSB.org]</ref> Histone Acetyltransferase Hpa2 is found in the organism Saccharomyces Cerevisiae, which is more commonly known as Baker's Yeast.<ref>"Q06592 (HPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot." Unitprot.org. UniProtKB, 13 Nov. 2013. Web. 16 Nov. 2013.[http://www.uniprot.org/uniprot/Q06592 UnitPro.org]</ref> 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.<ref name=desperate/><ref name=Shiva/> It is classified as a transferase.<ref name=Shiva>Angus-Hill, et al. "Crystal Structure of the Histone Acetyltransferase Hpa2: a Tetrameric Member of the Gcn5-related N-acetyltransferase Superfamily." J. Mol. Biol. 1999.3338 (1999): 1-14. Web. 18 Nov. 2013.</ref>
 =Structure=
-Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA)<ref name=Shiva/>. The method used to determine the structure was [[X-ray crystallography]]. Sedimentation and crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The crystal structure of the oligomer reveals that two Hpa2 dimers are held together by interaction between the bound acetyl-CoA molecules. The average B-factor value is 23.9 (<scene name='56/564050/Bakhbone_mainechain/1'>main chain</scene>) with a 25.4 <scene name='56/564050/Sidechain/2'>side chain</scene>. The R-factor is 0.19 <ref name=Shiva/>. Core fold features include four conserved sequence motifs of the GNAT family and comprises a central highly curved five stranded <scene name='56/564050/Beta_sheets/1'>Beta sheets</scene> (β1-β5) surrounded on both sides by helical segments (α1 and α3)<ref name=Shiva/>.
+Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA).<ref name=Shiva/> The method used to determine the structure was [[X-ray crystallography]]. Sedimentation and crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The crystal structure of the oligomer reveals that two Hpa2 dimers are held together by interaction between the bound acetyl-CoA molecules. The average B-factor value is 23.9 (<scene name='56/564050/Bakhbone_mainechain/1'>main chain</scene>) with a 25.4 <scene name='56/564050/Sidechain/2'>side chain</scene>. The R-factor is 0.19. <ref name=Shiva/> Core fold features include four conserved sequence motifs of the GNAT family and comprises a central highly curved five stranded <scene name='56/564050/Beta_sheets/1'>Beta sheets</scene> (β1-β5) surrounded on both sides by helical segments (α1 and α3).<ref name=Shiva/>
 =Secondary Structure=