|
Type |
Poster Presentation |
Area |
Physical Chemistry |
Room No. |
Event Hall |
Time |
4월 20일 (금요일) 11:00~12:30 |
Code |
PHYS.P-232 |
Subject |
Investigating Conformational Change of Sub-domain to Understand Structural Dynamics of Entire Oligomer in PixD (Slr1694) Protein |
Authors |
Sang Jin Lee, Yunbeom Lee, Hyotcherl Ihee* Department of Chemistry, Korea Advanced Institute of Science and Technology, Korea |
Abstract |
PixD is a protein associated with phototaxis mechanism in the cyanobacterium Synechocys. The PixD absorbs blue light as stimuli by BLUF (Blue Light Receptor Using Flavin chromophore) domain, and controls the phototaxis mechanism through signal transduction pathway caused by its structural change. In the natural world, PixD has a unique structure in which five PixD dimers form donut-shaped decamer. Due to this structural characteristic, the structural dynamics of PixD decamer starts from structural change of the PixD dimer. Here, we perform a solution X-ray scattering experiment about PixD dimer M93A mutant type to investigate how the structural change spreads to entire PixD decamer from PixD dimer. From the experiment, the structure of PixD dimer is changed by helix motion, and the pattern of change seems to be in the direction of increasing volume of PixD dimer. This result suggests that the volume expansion of PixD dimer causes entire structural dynamics of PixD decamer. |
E-mail |
sangj430@gmail.com |
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