1OSM | Outer Membrane Protein | date | Jan 08, 1999 |
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title | Osmoporin (Ompk36) From Klebsiella Pneumoniae | ||||||||||||||
authors | R.Dutzler, T.Schirmer | ||||||||||||||
compound | source | ||||||||||||||
Molecule: Ompk36 Chain: A, B, C Synonym: Osmoporin Engineered: Yes |
Organism_scientific: Klebsiella Pneumoniae Expression_system: Escherichia Coli | ||||||||||||||
symmetry | Space Group: C 1 2 1 | R_factor | 0.208 | ||||||||||||
crystal cell |
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method | X-Ray Diffraction | resolution | 3.20 Å | ||||||||||||
ligand | D12 | enzyme |
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similarity | Belongs to the gram-negative porin family.[Porin_1] | ||||||||||||||
subunit | Homotrimer. | ||||||||||||||
subcellular loc. |
Membrane localization by OPM: Bacterial gram-negative outer membrane
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Genes | OMPC, OMPK36 (K. pneumoniae) | ||||||||||||||
function | Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. In k.pneumoniae it has been shown to bind the c1q component and activate the classical pathway of the complement system. | ||||||||||||||
Gene Ontology |
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Primary reference | Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae., Dutzler R, Rummel G, Alberti S, Hernandez-Alles S, Phale P, Rosenbusch J, Benedi V, Schirmer T, Structure Fold Des 1999 Apr 15;7(4):425-34. PMID:10196126 |
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Structure-derived information |
- Domain d1osma_, region A [Jmol] [rasmolscript] [script source] - Domain d1osmb_, region B [Jmol] [rasmolscript] [script source] - Domain d1osmc_, region C [Jmol] [rasmolscript] [script source] |
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