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PDBsum entry 1mpr
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protein metals Protein-protein interface(s) links
Membrane protein PDB id
1mpr

 

 

 

 

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Contents
Protein chains
421 a.a. *
Metals
_CA
Waters ×456
* Residue conservation analysis
PDB id:
1mpr
Name: Membrane protein
Title: Maltoporin from salmonella typhimurium
Structure: Maltoporin. Chain: a, b, c. Synonym: lam-b, mal-l
Source: Salmonella typhimurium. Organism_taxid: 602. Strain: sl3749. Cellular_location: outer membrane
Biol. unit: Homo-Trimer (from PDB file)
Resolution:
2.80Å     R-factor:   0.183     R-free:   0.211
Authors: J.E.W.Meyer,G.E.Schulz
Key ref:
J.E.Meyer et al. (1997). Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J Mol Biol, 266, 761-775. PubMed id: 9102468 DOI: 10.1006/jmbi.1996.0823
Date:
18-Dec-96     Release date:   12-Mar-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P26466  (LAMB_SALTY) -  Maltoporin from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Seq:
Struc: 		452 a.a.
421 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1006/jmbi.1996.0823 J Mol Biol 266:761-775 (1997)
PubMed id: 9102468  
 
 
Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside.
J.E.Meyer, M.Hofnung, G.E.Schulz.
 
  ABSTRACT  
 
The maltodextrin-specific (malto-)porin from Salmonella typhimurium has been crystallized. Its three-dimensional structure was determined at 2.4 A resolution (1 A = 0.1 nm). A comparison with the structure of the homologous porin from Escherichia coli as well as with the sequences of other related porins showed that there are regions of appreciable sequence and structure variability, despite close overall similarity. The maltoporin structure was analyzed with a bound nitrophenyl-maltotrioside as well as without ligand. Maltotrioside binding had a negligible effect on the polypeptide structure. It binds at the pore eyelet assuming a conformation close to the natural amylose helix.
 
  Selected figure(s)  
 
Figure 6.
Figure 6. Stereo view of the interface around the molecular 3-fold axis. There is a water cluster in the interior and one calcium ion held by three aspartate residues at the external end of the interface (top). Because the respective residues are conserved, these features occur most likely also in the E. coli homologue. 		Figure 8.
Figure 8. Superposition of C^α backbones of maltoporin from S. typhimurium (black) and its homologue from E. coli (red). Some loops at the external end of the β-barrel are labeled. There is no electron density at the tip of loop L6, indicating high mobility.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1997, 266, 761-775) copyright 1997.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18849407 R.G.Coleman, and K.A.Sharp (2009).
Finding and characterizing tunnels in macromolecules with application to ion channels and pores.
  Biophys J, 96, 632-645.  
16424900 I.Iacovache, P.Paumard, H.Scheib, C.Lesieur, N.Sakai, S.Matile, M.W.Parker, and F.G.van der Goot (2006).
A rivet model for channel formation by aerolysin-like pore-forming toxins.
  EMBO J, 25, 457-466.  
16888630 O.Yildiz, K.R.Vinothkumar, P.Goswami, and W.Kühlbrandt (2006).
Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation.
  EMBO J, 25, 3702-3713.
PDB codes: 2iwv 2iww
17947032 R.Jackups, and J.Liang (2006).
Combinatorial model for sequence and spatial motif discovery in short sequence fragments: examples from beta-barrel membrane proteins.
  Conf Proc IEEE Eng Med Biol Soc, 1, 3470-3473.  
16434398 U.Zachariae, T.Klühspies, S.De, H.Engelhardt, and K.Zeth (2006).
High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32.
  J Biol Chem, 281, 7413-7420.
PDB codes: 2fgq 2fgr
15647112 P.G.Bagos, T.D.Liakopoulos, and S.J.Hamodrakas (2005).
Evaluation of methods for predicting the topology of beta-barrel outer membrane proteins and a consensus prediction method.
  BMC Bioinformatics, 6, 7.  
  15215418 F.S.Berven, K.Flikka, H.B.Jensen, and I.Eidhammer (2004).
BOMP: a program to predict integral beta-barrel outer membrane proteins encoded within genomes of Gram-negative bacteria.
  Nucleic Acids Res, 32, W394-W399.  
15141026 H.R.Bigelow, D.S.Petrey, J.Liu, D.Przybylski, and B.Rost (2004).
Predicting transmembrane beta-barrels in proteomes.
  Nucleic Acids Res, 32, 2566-2577.  
14978719 M.M.Gromiha, S.Ahmad, and M.Suwa (2004).
Neural network-based prediction of transmembrane beta-strand segments in outer membrane proteins.
  J Comput Chem, 25, 762-767.  
15162482 N.K.Natt, H.Kaur, and G.P.Raghava (2004).
Prediction of transmembrane regions of beta-barrel proteins using ANN- and SVM-based methods.
  Proteins, 56, 11-18.  
12835320 C.Danelon, T.Brando, and M.Winterhalter (2003).
Probing the orientation of reconstituted maltoporin channels at the single-protein level.
  J Biol Chem, 278, 35542-35551.  
12719230 G.Schwarz, C.Danelon, and M.Winterhalter (2003).
On translocation through a membrane channel via an internal binding site: kinetics and voltage dependence.
  Biophys J, 84, 2990-2998.  
12704154 S.Galdiero, D.Capasso, M.Vitiello, M.D'Isanto, C.Pedone, and M.Galdiero (2003).
Role of surface-exposed loops of Haemophilus influenzae protein P2 in the mitogen-activated protein kinase cascade.
  Infect Immun, 71, 2798-2809.  
11964234 F.Orlik, C.Andersen, and R.Benz (2002).
Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (Maltoporin) channel of Escherichia coli. I. Effect on ion transport.
  Biophys J, 82, 2466-2475.  
12080122 F.Orlik, C.Andersen, and R.Benz (2002).
Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (maltoporin) channel of Escherichia coli. II. Effect on maltose and maltooligosaccharide binding kinetics.
  Biophys J, 83, 309-321.  
12003940 P.Van Gelder, F.Dumas, I.Bartoldus, N.Saint, A.Prilipov, M.Winterhalter, Y.Wang, A.Philippsen, J.P.Rosenbusch, and T.Schirmer (2002).
Sugar transport through maltoporin of Escherichia coli: role of the greasy slide.
  J Bacteriol, 184, 2994-2999.  
12220498 R.Dutzler, T.Schirmer, M.Karplus, and S.Fischer (2002).
Translocation mechanism of long sugar chains across the maltoporin membrane channel.
  Structure, 10, 1273-1284.  
11790840 W.C.Wimley (2002).
Toward genomic identification of beta-barrel membrane proteins: composition and architecture of known structures.
  Protein Sci, 11, 301-312.  
12192075 Y.Zhai, and M.H.Saier (2002).
The beta-barrel finder (BBF) program, allowing identification of outer membrane beta-barrel proteins encoded within prokaryotic genomes.
  Protein Sci, 11, 2196-2207.  
11274469 I.Jacoboni, P.L.Martelli, P.Fariselli, V.De Pinto, and R.Casadio (2001).
Prediction of the transmembrane regions of beta-barrel membrane proteins with a neural network-based predictor.
  Protein Sci, 10, 779-787.  
11371453 T.Páli, and D.Marsh (2001).
Tilt, twist, and coiling in beta-barrel membrane proteins: relation to infrared dichroism.
  Biophys J, 80, 2789-2797.  
10692155 A.Charbit, C.Andersen, J.Wang, B.Schiffler, V.Michel, R.Benz, and M.Hofnung (2000).
In vivo and in vitro studies of transmembrane beta-strand deletion, insertion or substitution mutants of the Escherichia coli K-12 maltoporin.
  Mol Microbiol, 35, 777-790.  
10981633 G.E.Schulz (2000).
beta-Barrel membrane proteins.
  Curr Opin Struct Biol, 10, 443-447.  
10601863 H.Lång, M.Mäki, A.Rantakari, and T.K.Korhonen (2000).
Characterization of adhesive epitopes with the OmpS display system.
  Eur J Biochem, 267, 163-170.  
10973056 J.A.Killian, and G.von Heijne (2000).
How proteins adapt to a membrane-water interface.
  Trends Biochem Sci, 25, 429-434.  
10966478 J.L.Popot, and D.M.Engelman (2000).
Helical membrane protein folding, stability, and evolution.
  Annu Rev Biochem, 69, 881-922.  
10839820 M.H.Saier (2000).
A functional-phylogenetic classification system for transmembrane solute transporters.
  Microbiol Mol Biol Rev, 64, 354-411.  
10931321 R.Koebnik, K.P.Locher, and P.Van Gelder (2000).
Structure and function of bacterial outer membrane proteins: barrels in a nutshell.
  Mol Microbiol, 37, 239-253.  
10961503 Van Gelder P, F.Dumas, and M.Winterhalter (2000).
Understanding the function of bacterial outer membrane channels by reconstitution into black lipid membranes
  Biophys Chem, 85, 153-167.  
10027967 C.Andersen, B.Rak, and R.Benz (1999).
The gene bglH present in the bgl operon of Escherichia coli, responsible for uptake and fermentation of beta-glucosides encodes for a carbohydrate-specific outer membrane porin.
  Mol Microbiol, 31, 499-510.  
10361287 C.Andersen, C.Bachmeyer, H.Täuber, R.Benz, J.Wang, V.Michel, S.M.Newton, M.Hofnung, and A.Charbit (1999).
In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K-12 maltoporin: contribution to maltose and maltooligosaccharide transport and binding.
  Mol Microbiol, 32, 851-867.  
  10074088 C.Ulmke, J.Kreth, J.W.Lengeler, W.Welte, and K.Schmid (1999).
Site-directed mutagenesis of loop L3 of sucrose porin ScrY leads to changes in substrate selectivity.
  J Bacteriol, 181, 1920-1923.  
10611277 K.E.McAuley, P.K.Fyfe, J.P.Ridge, N.W.Isaacs, R.J.Cogdell, and M.R.Jones (1999).
Structural details of an interaction between cardiolipin and an integral membrane protein.
  Proc Natl Acad Sci U S A, 96, 14706-14711.
PDB code: 1qov
  10548053 N.Nagano, E.G.Hutchinson, and J.M.Thornton (1999).
Barrel structures in proteins: automatic identification and classification including a sequence analysis of TIM barrels.
  Protein Sci, 8, 2072-2084.  
10410805 S.H.White, and W.C.Wimley (1999).
Membrane protein folding and stability: physical principles.
  Annu Rev Biophys Biomol Struct, 28, 319-365.  
10383757 S.M.Newton, J.D.Igo, D.C.Scott, and P.E.Klebba (1999).
Effect of loop deletions on the binding and transport of ferric enterobactin by FepA.
  Mol Microbiol, 32, 1153-1165.  
9808047 A.Pautsch, and G.E.Schulz (1998).
Structure of the outer membrane protein A transmembrane domain.
  Nat Struct Biol, 5, 1013-1017.
PDB code: 1bxw
9437417 B.K.Jap, and P.J.Walian (1998).
Gliding through sugar channels: how sweet it is!
  Nat Struct Biol, 5, 6-8.  
9437428 D.Forst, W.Welte, T.Wacker, and K.Diederichs (1998).
Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose.
  Nat Struct Biol, 5, 37-46.
PDB codes: 1a0s 1a0t
9635733 D.P.Tieleman, and H.J.Berendsen (1998).
A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer.
  Biophys J, 74, 2786-2801.  
10089518 H.Kim (1998).
Crystallization of OmpC osmoporin from Escherichia coli.
  Acta Crystallogr D Biol Crystallogr, 54, 1399-1400.  
9437421 P.C.Preusch, J.C.Norvell, J.C.Cassatt, and M.Cassman (1998).
Progress away from 'no crystals, no grant'.
  Nat Struct Biol, 5, 12-14.  
10066479 P.E.Klebba, and S.M.Newton (1998).
Mechanisms of solute transport through outer membrane porins: burning down the house.
  Curr Opin Microbiol, 1, 238-247.  
9751640 R.M.Garavito (1998).
Membrane protein structures: the known world expands.
  Curr Opin Biotechnol, 9, 344-349.  
  9529892 W.Boos, and H.Shuman (1998).
Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation.
  Microbiol Mol Biol Rev, 62, 204-229.  
9778346 W.M.Yau, W.C.Wimley, K.Gawrisch, and S.H.White (1998).
The preference of tryptophan for membrane interfaces.
  Biochemistry, 37, 14713-14718.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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