Sandbox Reserved 774: Difference between revisions
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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 forms a loop before and around the first turn of the helix in Motif A. This is found in residues | 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 forms a loop before and around the first turn of the helix in Motif A. This is found in residues | ||
<scene name='56/564050/Residues_100-104/3' target=0>100-104</scene>. Most of the residues in this loop contribute to a series of hydrogen bonds between the Alpha and Beta phosphate oxygen atoms via main-chain groups. This includes a conserved solvent molecule interaction. This loops was not located within Hpa2 in the absence of its co-factor, indicating that this region is formed upon co-factor binding. It appears that this area of interactions is a vital determinant for the binding of AcCoA. <ref name=Shiva/> | <scene name='56/564050/Residues_100-104/3' target=0>100-104</scene>. Most of the residues in this loop contribute to a series of hydrogen bonds between the Alpha and Beta phosphate oxygen atoms via main-chain groups. This includes a conserved solvent molecule interaction. This loops was not located within Hpa2 in the absence of its co-factor, indicating that this region is formed upon co-factor binding. It appears that this area of interactions is a vital determinant for the binding of AcCoA. <ref name=Shiva/> | ||
==Active Site== | |||
The region around the <scene name='56/564050/Active_sites_zoom/1' target=1>active site</scene> has potential consequences for substrate binding. For Hpa2, there exists a pocket adjacent to the active site which is sealed off on two sides by the second Hpa2 monomer in each dimer. This pocket restricts the conformation of a polypeptide backbone in the vicinity of the active site. Therefore, Hpa2 is able to distinguish between potential substrate, whereby the only lysine side-chains that may enter the active site are those with surrounding polypeptides that can adopt a conformation with the ability to fit through the pocket. <ref name=Shiva/> | |||
<Structure load='1QSM' size='300' frame='true' align='right' caption='Hpa2 + AcCoA' scene='Insert optional scene name here' /> | <Structure load='1QSM' size='300' frame='true' align='right' caption='Hpa2 + AcCoA' scene='Insert optional scene name here' /> | ||
=Secondary Structure= | =Secondary Structure= | ||
