RiAFP: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 1: Line 1:
<StructureSection load='4dt5' size='340' side='right' caption='Insect antifreeze protein complex with sulfate and glycerol (PDB code [[4dt5]]).' scene='60/607864/Chain_a_without_histag/1'>
<StructureSection load='4dt5' size='340' side='right' caption='Insect antifreeze protein complex with sulfate and glycerol (PDB code [[4dt5]]).' scene='60/607864/Chain_a_without_histag/1'>
Antifreeze proteins (AFPs) evolved in various organisms permitting their survival in subzero environments<ref>PMID: 11852248</ref>. They exhibit remarkable structural diversity and molar activities across the various kingdoms<ref>10.5772/54992</ref>. The longhorn beetle, Rhagium inquisitor, has the ability to supercool to below -25 °C partially due to the presence of a highly potent AFP (RiAFP) in its hemolymph. RiAFP is a 13-kDa protein with one of the highest antifreeze activities measured for any AFP.


Antifreeze proteins (AFPs) evolved in various organisms permitting their survival in subzero environments<ref>PMID: 11852248</ref>. They exhibit remarkable structural diversity and molar activities across the various kingdoms<ref>10.5772/54992</ref>. The longhorn beetle, Rhagium inquisitor, has the ability to supercool to below -25 °C partially due to the presence of a highly potent AFP (RiAFP) in its hemolymph. RiAFP is a 13-kDa protein with one of the highest antifreeze activities measured for any AFP.
== History ==


== Overall Structure ==
== Overall Structure ==
Line 10: Line 11:
== Ice Binding Surface (IBS) ==
== Ice Binding Surface (IBS) ==
IBS of RiAFP contains five expanded <scene name='60/607864/Ibs/1'>TXTXTXT motifs</scene> within the top (blue) β–sheet. These motifs are remarkably regular, allowing any rows/columns of TXTXTXT motifs to be exactly superposed onto any other rows/columns. Threonine residuses are crucial for maintaining antifreeze activity. It was found in other AFPs that mutations of the Thrs within these motifs decrease the thermal hysteresis. The Thr hydroxyls define a large flat IBS of 420 Å2, which correlates with high antifreeze activity.
IBS of RiAFP contains five expanded <scene name='60/607864/Ibs/1'>TXTXTXT motifs</scene> within the top (blue) β–sheet. These motifs are remarkably regular, allowing any rows/columns of TXTXTXT motifs to be exactly superposed onto any other rows/columns. Threonine residuses are crucial for maintaining antifreeze activity. It was found in other AFPs that mutations of the Thrs within these motifs decrease the thermal hysteresis. The Thr hydroxyls define a large flat IBS of 420 Å2, which correlates with high antifreeze activity.
== Molecular Basis for Ice Binding ==


== Function ==
== Function ==