Average images from GroEL side views in the absenceorpresence
of ADP and GroES. Escherichia coli GroEL and GroES are the
prototypical chaperonin and co-chaperonin. Chaperonins
arering-shaped molecular chaperone proteins that are found
in all organisms and are essential for protein
folding and protection from stress. Both the
chaperonin and co-chaperonin are 7-fold symmetric
oligomers. GroEL is composed of fourteen identical 60
kDa subunits arranged in two stacked rings, and
GroES is composed of a seven identical 10 kDa subunits.
1. Show the crystal structure of a single GroES subunit.
restrict carbon
strabds
restrict :O
color structure
zoom 250
2. Show the crystal structure of a single GroEL subunit.
restrict carbon
strands
restrict :a
color structure
zoom 250
3. Show "top view" C-alpha trace colored by chain of GroEL
and measure the width of its central cavities.
restrict carbon
backbone 0.3
restrict :a or :b or :c or :d or :e or :f or :g
select :*
color *
set picking distance
zoom 160
4. Show "side view" cartoon display colored by structure
of GroES and measure its width.
restrict carbon
cartoons
restrict :o or :p or :q or :r or :s or :t or :u
color structure
center glu50:t
rotate x 270
zoon 200
set picking distance
color labels blue
5. Estimate the central cavities' width of GroEL from image shown above.
Compare this width with the one you measured from crystal structure.
Ans:
The width of above images is 5.0 nm,
It is 4.5nm in width of crystal structure my measured.