2fgr: Difference between revisions
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|PDB= 2fgr |SIZE=350|CAPTION= <scene name='initialview01'>2fgr</scene>, resolution 1.500Å | |PDB= 2fgr |SIZE=350|CAPTION= <scene name='initialview01'>2fgr</scene>, resolution 1.500Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1e54|1E54]], [[2fgq|2FGQ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fgr OCA], [http://www.ebi.ac.uk/pdbsum/2fgr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fgr RCSB]</span> | |||
}} | }} | ||
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[[Category: Zachariae, U.]] | [[Category: Zachariae, U.]] | ||
[[Category: Zeth, K.]] | [[Category: Zeth, K.]] | ||
[[Category: omp32 porin outer membrane protein]] | [[Category: omp32 porin outer membrane protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:02:32 2008'' | ||
Revision as of 03:02, 31 March 2008
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| , resolution 1.500Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1E54, 2FGQ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
High resolution Xray structure of Omp32
OverviewOverview
The porin Omp32 is the major outer membrane protein of the bacterium Delftia acidovorans. The crystal structures of the strongly anion-selective porin alone and in complex with the substrate malate were solved at 1.5 and 1.45 A resolution, respectively, and revealed a malate-binding motif adjacent to the channel constriction zone. Binding is mediated by interaction with a cluster of two arginine residues and two threonines. This binding site is specific for Omp32 and reflects the physiological adaptation of the organism to organic acids. Structural studies are combined with a 7-ns unbiased molecular dynamics simulation of the trimeric channel in a model membrane. Molecular dynamics trajectories show how malate ions are efficiently captured from the surrounding bulk solution by the electrostatic potential of the channel, translocated to the binding site region, and immobilized in the constriction zone. In accordance with these results, conductance measurements with Omp32 inserted in planar lipid membranes revealed binding of malate. The anion-selective channel Omp32 is the first reported example of a porin with a 16-stranded beta-barrel and proven substrate specificity. This finding suggests a new view on the correlation of porin structure with substrate binding in specific channels.
About this StructureAbout this Structure
2FGR is a Single protein structure of sequence from Delftia acidovorans. Full crystallographic information is available from OCA.
ReferenceReference
High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32., Zachariae U, Kluhspies T, De S, Engelhardt H, Zeth K, J Biol Chem. 2006 Mar 17;281(11):7413-20. Epub 2006 Jan 23. PMID:16434398
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