carbohydrate porin belonging to the LamB family whose members are thought to bind various sugars; similar to maltoporin which is involved in the transport of maltose and maltodextrins
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the ...
125-538
1.06e-106
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the diffusion of maltodextrins and other sugars across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an 18-strand antiparallel beta-barrel (18,22). Loop 3 folds into the core to constrict pore size. Long irregular loops are found on the extracelllular side, while short turns are in the periplasm.Tightly-bound water molecules are found in the eyelet of the passage, and only substrates that can displace and replace the broken hydrogen bonds are likely to enter the pore. In the MPR structure, loops 4,6, and 9 have the greatest mobility and are highly variable; these are postulated to attract maltodextrins.
:
Pssm-ID: 238656 Cd Length: 392 Bit Score: 324.72 E-value: 1.06e-106
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, ...
27-57
4.26e-11
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, N-terminal extension of the outer membrane maltoporins, pfam02264, LamB.
:
Pssm-ID: 431901 Cd Length: 31 Bit Score: 57.65 E-value: 4.26e-11
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the ...
125-538
1.06e-106
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the diffusion of maltodextrins and other sugars across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an 18-strand antiparallel beta-barrel (18,22). Loop 3 folds into the core to constrict pore size. Long irregular loops are found on the extracelllular side, while short turns are in the periplasm.Tightly-bound water molecules are found in the eyelet of the passage, and only substrates that can displace and replace the broken hydrogen bonds are likely to enter the pore. In the MPR structure, loops 4,6, and 9 have the greatest mobility and are highly variable; these are postulated to attract maltodextrins.
Pssm-ID: 238656 Cd Length: 392 Bit Score: 324.72 E-value: 1.06e-106
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the ...
128-538
2.59e-105
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel.
Pssm-ID: 426687 Cd Length: 385 Bit Score: 320.79 E-value: 2.59e-105
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, ...
27-57
4.26e-11
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, N-terminal extension of the outer membrane maltoporins, pfam02264, LamB.
Pssm-ID: 431901 Cd Length: 31 Bit Score: 57.65 E-value: 4.26e-11
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the ...
125-538
1.06e-106
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the diffusion of maltodextrins and other sugars across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an 18-strand antiparallel beta-barrel (18,22). Loop 3 folds into the core to constrict pore size. Long irregular loops are found on the extracelllular side, while short turns are in the periplasm.Tightly-bound water molecules are found in the eyelet of the passage, and only substrates that can displace and replace the broken hydrogen bonds are likely to enter the pore. In the MPR structure, loops 4,6, and 9 have the greatest mobility and are highly variable; these are postulated to attract maltodextrins.
Pssm-ID: 238656 Cd Length: 392 Bit Score: 324.72 E-value: 1.06e-106
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the ...
128-538
2.59e-105
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel.
Pssm-ID: 426687 Cd Length: 385 Bit Score: 320.79 E-value: 2.59e-105
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, ...
27-57
4.26e-11
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, N-terminal extension of the outer membrane maltoporins, pfam02264, LamB.
Pssm-ID: 431901 Cd Length: 31 Bit Score: 57.65 E-value: 4.26e-11
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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