Sandbox Reserved 774: Difference between revisions
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Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a <scene name='56/564050/Test/1' target=1>co-factor</scene> (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 <scene name='56/564050/Test/1' target=1>co-factor</scene> (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/> | ||
<Structure load='1QSM' size='300' frame='true' align='right' caption=' | ==Co-factor== | ||
Most of the hydrogen bonding between Hpa2 and its co-factor AcCoA are highly conserved and occur via the main-chain groups, not the side-chains. This explains the uniformity of the binds with the co-factors, despite the low degree of sequence conservation. The conserved main-chain contacts seen in a segment of Motif A form loops before and around the first turn of the helix in Motif A. This is found in residues | |||
<scene name='56/564050/Residues_100-104/1' target=0>100-104.</scene><ref name=Shiva/> | |||
<Structure load='1QSM' size='300' frame='true' align='right' caption='Hpa2 + AcCoA' scene='Insert optional scene name here' /> | |||
=Secondary Structure= | =Secondary Structure= | ||
