Lecture 9 B prop

Question 1

How is stability in B-propellers conferred?

Answer 1

Molecular velcro- mainchain H-bonds
face to face

Structural rigidity

Question 2

Paper points

Answer 2

Their central tunnel is typically funnel-shaped and lined with hydrogen donors and acceptors from the edges of inner b strands;

Question 3

extra reading WD domain

Answer 3

Perhaps the most remarkable feature of some b -propeller proteins is the relative clarity with which repeating structural features appear in the sequence WD-repeat motif WD repeat corresponds to the first three strands of one blade and the last strand of the next blade.

Question 4

How are hydrogen bonds big in B propellor

Answer 4

b-propeller domain are in a fully stretched conformation, with radially directed hydrogen bonds.mainchain hydrogen bonds are accessible at the surface of the propeller and can influence interactions with other protein/substrate molecules two subunits

within the dimer of cytochrome cd1 are held together by mainchain hydrogen bonds between the propeller (d1) domains that extend from one monomer to the other (Figure 1).

Question 5

Specificity in b propellors

Answer 5

How the protein folds

proyl oligopeptidase family- 2

Question 6

how is specificity conferred

Answer 6

As the
-sheets pack into the circular array, a tunnel is formed through the centre of the propeller
conical in shape
In the case ofprolyl oligopeptidase, the tunnel regulates substrate access to an active site formed at the interface between two domains

Question 7

How is the folds controlled extra reading

Answer 7

Functional diversity

No Velcro system has been found in the 7-bladed non catalytic domain of prolyl oligopeptidase propeller domain is actually topologically inserted into the catalytic hydrolase domain. the occurrence ofthese aspartate residues and their interactions across the structures ofthe distinct 7-bladed proteins is likely to be important for the fold.