Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
| Autor: | Kay Diederichs, Doris Forst, Thomas Wacker, Wolfram Welte |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
Salmonella typhimurium
Salmonella Sucrose Multiple isomorphous replacement Stereochemistry Molecular Sequence Data Maltoporin Porins Trimer medicine.disease_cause Crystallography X-Ray Biochemistry Microbiology chemistry.chemical_compound Bacterial Proteins Structural Biology ddc:570 Genetics medicine Amino Acid Sequence chemistry.chemical_classification Binding Sites Sequence Homology Amino Acid Membrane Proteins Biological Transport Hydrogen Bonding Amino acid Protein Structure Tertiary Monomer chemistry Solubility Porin Receptors Virus Sequence Alignment Bacterial Outer Membrane Proteins Protein Binding |
| Popis: | The X-ray structure of a sucrose-specific porin (ScrY) from Salmonella typhimurium has been determined by multiple isomorphous replacement at 2.4 A resolution both in its uncomplexed form and with bound sucrose. ScrY is a noncrystallographic trimer of identical subunits, each with 413 structurally well-defined amino acids. A monomer is built up of 18 anti-parallel beta-strands surrounding a hydrophilic pore, with a topology closely similar to that of maltoporin. Two non-overlapping sucrose-binding sites were identified in difference Fourier maps. The higher permeability for sucrose of ScrY as compared to maltoporin is mainly accounted for by differences in their pore-lining residues. |
| Databáze: | OpenAIRE |
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