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| [[Image:2ffb.gif|left|200px]] | | {{Seed}} |
| | [[Image:2ffb.png|left|200px]] |
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| {{STRUCTURE_2ffb| PDB=2ffb | SCENE= }} | | {{STRUCTURE_2ffb| PDB=2ffb | SCENE= }} |
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| '''The crystal structure of the HlyB-NBD E631Q mutant in complex with ADP'''
| | ===The crystal structure of the HlyB-NBD E631Q mutant in complex with ADP=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_16858415}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16858415 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16858415}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Abc-transporter]] | | [[Category: Abc-transporter]] |
| [[Category: Atpase]] | | [[Category: Atpase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:49:37 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:54:27 2008'' |
