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In silico Simulations of E. coli HslVU to Explore B. subtilis CodWX Structure

Submission Date :
2 / 24 / 2006 , 18 : 11 : 51
Abstract Number :
Presenting Type:
Poster Presentation
Presenting Area :
Authors :
K.Navaneethakrishnan, Liu Shui, 이근우
경상대학교 생화학과,
Assigned Code :
31P304포 Assigend Code Guideline
Presenting Time :
금 <발표Ⅱ>
Proteasomes are multicatalytic proteolytic complexes present in all eukaryotic cells. The 26S type of the proteasome catalyzes the degradation of ubiquitin conjugated proteins, and thus it plays a key role in many cellular processes. In 1995, 20S proteasomes were discovered in the actinomycete Rhodococcus, and in the Escherichia coli genome sequencing project, a novel Heat-shock locus (HslVU) was discovered that encodes a 19-kDa protein (HslV), whose sequence is 20% similar to 3-type proteasome beta subunits and a conserved fold. CodW and CodX, encoded by the cod operon in Bacillus subtilis, display 52% identity in their amino acid sequences to HslV and HslU in E.coli respectively. CodX and CodW can function together as a new type of two-component ATP-dependent protease. Therefore, understanding the dynamics of these protein regions are of importance. As the dynamic behavior of proteins depends on its native environment, in Silico simulations of HslVU have been done in polar environment. The simulations, done at the level of the dimmer of HslV and U complex with ATP are analyzed.