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The most frequent of the domain structures are the 
α/β domains 
 a central parallel or mixed β sheet surrounded by 
α helices 
 binding crevices are formed by loop regions. 
do not contribute to the structural stability of the 
fold 
but participate in binding and catalytic action.
CLASSES OF α/β PROTEINS 
 All glycolytic enzymes are α/β structures 
 3 main classes 
 TIM BARREL 
 ROSSMAN FOLD 
 HORSE SHOE FOLD
TIM BARREL 
 Barrel of beta sheets 
 Surrounded by alpha helices 
 Beta sheets form the core 
 Eg: Triosephosphate isomerase
ROSSMAN FOLD 
 Michel Rossman, 1970 
 Lactate dehydrogenase 
 Open twisted sheet with 
helices on both sides
HORSESHOE FOLD 
 Leucine rich motifs 
 Curved parallel beta sheets 
with 
all alpha helices on the outside 
 Eg: Ribonuclease inhibitor
ACTIVE SITE IN BARRELS 
 Formed by loops at one end of the α/β barrel 
 Active site 
Situated in the bottom 
Funnel-shaped pocket 
Created by 8 loops 
Connect the C terminal of beta sheets with N terminal of 
alpha helices 
(Ref toozen and branden page 53)
POSITIONS OF ACTIVE SITES 
 General relationship b/w structure & function of 
alpha/beta structures 
 Active site @ same position- w r t their common 
structure- inspite of having diff. functions & diff. aa 
sequences 
 Barrel structures – funnel shaped active site 
 Open α/β structures- crevices at the edge of beta 
sheets. 
 Crevice- formed by 2 adjacent loop regions that 
connect the 2 strands with alpha helices on opp.sides 
of beta sheet.
Two β-α-β motifs can be joined into a 
four-stranded parallel β sheet in two 
different ways
EXAMPLES 
 Some of the crucial enzymes formed by α/β structures 
Flavodoxin- has binding site for FMN(flavin 
mononucleotide) 
Adenylate kinase- AMP binding site 
Tyrosyl tRNA synthetase- protein synthesis 
Carboxypeptidases- hydrolysis of polypeptides at C 
terminal position 
Arabinose binding protein-transport of sugars, aa, 
ions…in Gram negative bacteria
Alpha/beta domains

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Alpha/beta domains

  • 1.
  • 2. The most frequent of the domain structures are the α/β domains  a central parallel or mixed β sheet surrounded by α helices  binding crevices are formed by loop regions. do not contribute to the structural stability of the fold but participate in binding and catalytic action.
  • 3. CLASSES OF α/β PROTEINS  All glycolytic enzymes are α/β structures  3 main classes  TIM BARREL  ROSSMAN FOLD  HORSE SHOE FOLD
  • 4. TIM BARREL  Barrel of beta sheets  Surrounded by alpha helices  Beta sheets form the core  Eg: Triosephosphate isomerase
  • 5. ROSSMAN FOLD  Michel Rossman, 1970  Lactate dehydrogenase  Open twisted sheet with helices on both sides
  • 6. HORSESHOE FOLD  Leucine rich motifs  Curved parallel beta sheets with all alpha helices on the outside  Eg: Ribonuclease inhibitor
  • 7. ACTIVE SITE IN BARRELS  Formed by loops at one end of the α/β barrel  Active site Situated in the bottom Funnel-shaped pocket Created by 8 loops Connect the C terminal of beta sheets with N terminal of alpha helices (Ref toozen and branden page 53)
  • 8. POSITIONS OF ACTIVE SITES  General relationship b/w structure & function of alpha/beta structures  Active site @ same position- w r t their common structure- inspite of having diff. functions & diff. aa sequences  Barrel structures – funnel shaped active site  Open α/β structures- crevices at the edge of beta sheets.  Crevice- formed by 2 adjacent loop regions that connect the 2 strands with alpha helices on opp.sides of beta sheet.
  • 9. Two β-α-β motifs can be joined into a four-stranded parallel β sheet in two different ways
  • 10. EXAMPLES  Some of the crucial enzymes formed by α/β structures Flavodoxin- has binding site for FMN(flavin mononucleotide) Adenylate kinase- AMP binding site Tyrosyl tRNA synthetase- protein synthesis Carboxypeptidases- hydrolysis of polypeptides at C terminal position Arabinose binding protein-transport of sugars, aa, ions…in Gram negative bacteria