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Slide 1. My name is Yoshitaka AISU. E-mail address: ( withheld ). Professor of my laboratory is Takahisa IKEGAMI. My research project is not already decided. But, I will research the structure of any proteins by NMR. - PowerPoint PPT Presentation
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My name is Yoshitaka AISU.
E-mail address: (withheld)
Professor of my laboratory is Takahisa IKEGAMI.
My research project is not already decided. But, I will research the structure of any proteins by NMR
The name of my protein is ADP-ribosylation factor 6 (ARF6) and its function is cell invasion.
PDB code is 2D1X.
Resolution is 1.90Å, R-Value 0.216, and R-free 0.226.
Slide 1
This report is made available with the kind permission of the student who prepared it, Yoshitaka Aisu. It was prepared for the 2010 class at Osaka University, Japan (workshops.molviz.org). The only change is that the student’s email address was removed, and this paragraph was added. Each slide answers a specific question.
Slide 2
six protein chains, no DNA, no RNA.
Ligands Three letter codes SO4 Full name SULFATE ION
Slide 3
Slide 4A
only beta sheet
there is no disulfide bond.
3KJ6
2 disulfide bonds within chain L 2 disulfide bonds within chain H
2 disulfide bonds between chain L and chain H
Slide 4B
Slide 5
There is a hydrophobic core.
Slide 6
This protein is soluble .
Slide 7
salt bridge and hydrogen bond
Slide 8
High conserved GLU21:A - expected
High conserved VAL57:A - unexpected
Because GLU21 is near the legand SO4.
Slide 9
Asymmetric unit Biological unit PISA
6 chains 6 chains
conformation is difference between the AU and PISA.Author’s biological unit is 3 chains.
Slide 10
List the gap in 2D1X
chain A : 1-6chain P : 1-2chain P : 12-15chain B : 1-7
chain Q : 1-2chain Q : 12-15chain D : 1-7
Slide 11
Sandbox Reserved 3
change colors
Slide 12
red: negative charge
blue: positive charge
Slide 13
Number of energetically significant ARG/TYR cation-pi interactions: 2
ARG42:A with TYR49:C ARG4:Q with TYR12:D
Slide 14
Residue of high temperature Glu1:C
Thank you for your lecture.
See you , again.
I enjoy leaning computer science.