Title: Protein Structures 2' Tertiary Structure
1Protein Structures2. Tertiary Structure
2Protein Tertiary Structure
- Packing
- helix-helix packing
- sheet-sheet packing
- helix-sheet packing
- Protein Structural Classes
- All Alpha
- All Beta
- Alpha and Beta
3Helix Helix Packing
The Ridge-Groove model
4Pairs of helices
W angle between the 2 axes
D distance between the two axes
5Two types of ridges in helices
Ridge 4n
Ridge 3n
6Ridge groove model for helix-helix packing
7Example Helix B and G in myoglobin
8Example Helix B and G in myoglobin
Backbone Sidechain
Backbone only
9Sheet-Sheet Packing
- Parallel sheets tend to be covered by helices on
both sides - Anti-parallel sheets tend to have one side
covered by a sheet sandwich-type structure.
Two types of packing aligned, or orthogonal
10Aligned sheet-sheet packing
Approx. 20 degrees between the directions of the
sheets
Sidechains are well packed
11Orthogonal Sheet-Sheet Packing
12Helix-Sheet Packing
- Because the periodicities of helices and strands
are different, there is not regular packing
patterns. - Helices tend to be on both sides of parallel beta
sheets.
13Protein Architectures
- All a proteins
- All b proteins
- Alpha and beta proteins
- - a/b proteins (alternating a and b)
- - a b proteins
14All-Alpha topologies
- The lone helix
- The helix-turn-helix motif
Glucagon (hormone involved Is regulating sugar
metabolism) PDB code 1GCN
ROP RNA-binding Protein PDB code 1ROP
The 2 helices are twisted
15All-Alpha topologies (2)
The four helix bundle
hydrophobic
hydrophilic
16Four helix bundle topologies
Rop dimer PDB 1ROP
Myohemerythrin PDB code 2mhr
17All Beta Topology
Beta sandwiches
Fatty acid binding protein PDB code 1IFB
18The Greek Key Topology
Folds including the Greek key topology include 5
to 13 strands.
19The Greek Key Topology
Gamma crystallin. PDB code 2GCR
20The Jellyroll Topology
A Greek key with an extra swirl
PDB code 2STV (coat protein of a virus)
21The Beta Propellor
Seven-plated propellor Each plate is a
four-stranded anti-parallel sheet PDB code 1ERJ
22The Beta Helix
PDB code 1EZG
Antifreeze protein from Tenebrio Molitor (beetle)
23The Rossman Fold
Alternate beta / alpha motif Always right handed
24The Horseshoe
PDB code 2BNH
25The alpha/beta barrel
In a succession of alpha/beta motifs, if the
first strand Hydrogen bonds to the last, then
the structure resemble a Barrel. PDB code 1TIM
26Summary
- Stacking of helices is best described using the
ridge-groove model. - Anti-parallel sheets tend to have one side
covered by a sheet sandwich-type structure.
Two types of packing aligned, or orthogonal. - Helices tend to be on both sides of parallel beta
sheets. - There are three main classes of proteins all
Alpha, all Beta and Alpha Beta. Sometimes, the
latter is divided in two, considering the
alternating alpha/beta proteins as defining their
own class. - Bundles are common alpha-proteins
- Common beta folds include the greek key, the
jellyroll, and sandwiches. More unusual beta
structures include the beta propeller and the
beta helix - The Rossman fold (alternating alpha/beta) is a
common motif in proteins. It is found in the
horseshoe, as well as in the TIM fold.