2fgk
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= hlyB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= hlyB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mt0|1MT0]], [[1xef|1XEF]], [[2fgj|2FGJ]], [[1ffa|1FFA]], [[1ffb|1FFB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fgk OCA], [http://www.ebi.ac.uk/pdbsum/2fgk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fgk RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Schmitt, L.]] | [[Category: Schmitt, L.]] | ||
[[Category: Zaitseva, J.]] | [[Category: Zaitseva, J.]] | ||
| - | [[Category: ATP]] | ||
[[Category: abc-cassette]] | [[Category: abc-cassette]] | ||
[[Category: abc-transporter]] | [[Category: abc-transporter]] | ||
[[Category: atp-loaded dimer]] | [[Category: atp-loaded dimer]] | ||
| - | ''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 03:02:27 2008'' |
Revision as of 00:02, 31 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | hlyB (Escherichia coli) | ||||||
| Related: | 1MT0, 1XEF, 2FGJ, 1FFA, 1FFB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the ABC-cassette E631Q mutant of HlyB with bound ATP
Overview
The ATP-binding cassette (ABC)-transporter haemolysin (Hly)B, a central element of a Type I secretion machinery, acts in concert with two additional proteins in Escherichia coli to translocate the toxin HlyA directly from the cytoplasm to the exterior. The basic set of crystal structures necessary to describe the catalytic cycle of the isolated HlyB-NBD (nucleotide-binding domain) has now been completed. This allowed a detailed analysis with respect to hinge regions, functionally important key residues and potential energy storage devices that revealed many novel features. These include a structural asymmetry within the ATP dimer that was significantly enhanced in the presence of Mg2+, indicating a possible functional asymmetry in the form of one open and one closed phosphate exit tunnel. Guided by the structural analysis, we identified two amino acids, closing one tunnel by an apparent salt bridge. Mutation of these residues abolished ATP-dependent cooperativity of the NBDs. The implications of these new findings for the coupling of ATP binding and hydrolysis to functional activity are discussed.
About this Structure
2FGK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer., Zaitseva J, Oswald C, Jumpertz T, Jenewein S, Wiedenmann A, Holland IB, Schmitt L, EMBO J. 2006 Jul 26;25(14):3432-43. Epub 2006 Jul 6. PMID:16858415
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