1mt0
From Proteopedia
(New page: 200px<br /><applet load="1mt0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mt0, resolution 2.6Å" /> '''ATP-binding domain of...) |
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| - | [[Image:1mt0.jpg|left|200px]]<br /><applet load="1mt0" size=" | + | [[Image:1mt0.jpg|left|200px]]<br /><applet load="1mt0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mt0, resolution 2.6Å" /> | caption="1mt0, resolution 2.6Å" /> | ||
'''ATP-binding domain of haemolysin B from Escherichia coli'''<br /> | '''ATP-binding domain of haemolysin B from Escherichia coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ABC-transporter haemolysin B is a central component of the secretion | + | The ABC-transporter haemolysin B is a central component of the secretion machinery that translocates the toxin, haemolysin A, in a Sec-independent fashion across both membranes of E. coli. Here, we report the X-ray crystal structure of the nucleotide-binding domain (NBD) of HlyB. The molecule shares the common overall architecture of ABC-transporter NBDs. However, the last three residues of the Walker A motif adopt a 3(10) helical conformation, stabilized by a bound anion. In consequence, this results in an unusual interaction between the Walker A lysine residue and the Walker B glutamate residue. As these residues are normally required to be available for ATP binding, for catalysis and for dimer formation of ABC domains, we suggest that this conformation may represent a latent monomeric form of the NBD. Surprisingly, comparison of available NBD structures revealed a structurally diverse region (SDR) of about 30 residues within the helical arm II domain, unique to each of the eight NBDs analyzed. As this region interacts with the transmembrane part of ABC-transporters, the SDR helps to explain the selectivity and/or targeting of different NBDs to their cognate transmembrane domains. |
==About this Structure== | ==About this Structure== | ||
| - | 1MT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MT0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Benabdelhak, H.]] | [[Category: Benabdelhak, H.]] | ||
| - | [[Category: Blight, M | + | [[Category: Blight, M A.]] |
| - | [[Category: Holland, I | + | [[Category: Holland, I B.]] |
[[Category: Schmitt, L.]] | [[Category: Schmitt, L.]] | ||
| - | [[Category: Stubbs, M | + | [[Category: Stubbs, M T.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: abc-transporter]] | [[Category: abc-transporter]] | ||
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[[Category: haemolysin b]] | [[Category: haemolysin b]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:43 2008'' |
Revision as of 11:58, 21 February 2008
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ATP-binding domain of haemolysin B from Escherichia coli
Overview
The ABC-transporter haemolysin B is a central component of the secretion machinery that translocates the toxin, haemolysin A, in a Sec-independent fashion across both membranes of E. coli. Here, we report the X-ray crystal structure of the nucleotide-binding domain (NBD) of HlyB. The molecule shares the common overall architecture of ABC-transporter NBDs. However, the last three residues of the Walker A motif adopt a 3(10) helical conformation, stabilized by a bound anion. In consequence, this results in an unusual interaction between the Walker A lysine residue and the Walker B glutamate residue. As these residues are normally required to be available for ATP binding, for catalysis and for dimer formation of ABC domains, we suggest that this conformation may represent a latent monomeric form of the NBD. Surprisingly, comparison of available NBD structures revealed a structurally diverse region (SDR) of about 30 residues within the helical arm II domain, unique to each of the eight NBDs analyzed. As this region interacts with the transmembrane part of ABC-transporters, the SDR helps to explain the selectivity and/or targeting of different NBDs to their cognate transmembrane domains.
About this Structure
1MT0 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains., Schmitt L, Benabdelhak H, Blight MA, Holland IB, Stubbs MT, J Mol Biol. 2003 Jul 4;330(2):333-42. PMID:12823972
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