Table 2 Position and distribution of Trp residues in structures of known transmembrane barrels

From: Differential Contribution of Tryptophans to the Folding and Stability of the Attachment Invasion Locus Transmembrane β-Barrel from Yersinia pestis

     

Position of Trp residued

S. No.a,b

PDB IDc

Proteina,b

# of β-strandsd,e

# of Trp residues

Membrane interface

Transmembrane

Extra-membrane

1

1P4T

NspA

10 (8)

0

-

-

-

2

2POR

Porin

22 (16)

1

1

-

-

3

3QRA

Ail

9 (8)

2

1

1

-

4

1QJ8

OmpX

8 (8)

2

1

1

-

5

2LHF

OprH

10 (8)

2

2

-

-

6

3HW9

OmpF

25 (16)

2

1

1

-

7

1E54

Omp32

24 (16)

2

-

1

1

8

3DZM

TtoA

14 (8)

3

1

-

2

9

3FID

LpxR

17 (12)

3

-

1

2

10

2X27

OprG

17 (8)

4

4

-

-

11

3BRY

TbuX

27 (14)

4

2

2

-

12

1K24

OpcA

15 (10)

4

3

1

-

13

1UYN

NalP

14 (12)

4

3

-

1

14

1H6S

Porin

19 (16)

4

3

1

-

15

3EMO

Hia

[6 (4)]x3f

1

1

-

-

16

4FQE

KdgM

14 (12)

3

2

-

1

17

1UUN

MspA

[14 (2)]x8f

4

3

1

-

18

3WI4

PorB

[22 (16)]x3f

4

3

-

1

19

1WP1

OprM

[13 (4)]x3f

4

2

-

2

20

2LME

YadA

[5 (4)]x3f

2

1

-

1

  1. aNon-redundant structures were retrieved from PDBTM: Protein Data Bank of Transmembrane Proteins; http://pdbtm.enzim.hu/. Only proteins with a maximum of four Trp residues are listed.
  2. bExamples 15-19 have been classified as porins in PDB; 20 is an anchor protein.
  3. cPDB: RCSB Protein Data Bank; http://www.rcsb.org/pdb.
  4. dInformation derived from both PDBTM and PDB.
  5. eNumbers provided represent the total number of β-strands in the structure and those in brackets represent the total number of transmembrane β-strands.
  6. f[Number of strands in one monomer (Number of transmembrane strands in one monomer)] x Number of monomers.
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