1l2t: Difference between revisions
New page: left|200px<br /><applet load="1l2t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2t, resolution 1.90Å" /> '''Dimeric Structure of... |
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[[Image:1l2t.gif|left|200px]]<br /><applet load="1l2t" size=" | [[Image:1l2t.gif|left|200px]]<br /><applet load="1l2t" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1l2t, resolution 1.90Å" /> | caption="1l2t, resolution 1.90Å" /> | ||
'''Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette'''<br /> | '''Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette'''<br /> | ||
==Overview== | ==Overview== | ||
It has been proposed that the reaction cycle of ATP binding cassette (ABC) | It has been proposed that the reaction cycle of ATP binding cassette (ABC) transporters is driven by dimerization of their ABC motor domains upon binding ATP at their mutual interface. However, no such ATP sandwich complex has been observed for an ABC from an ABC transporter. In this paper, we report the crystal structure of a stable dimer formed by the E171Q mutant of the MJ0796 ABC, which is hydrolytically inactive due to mutation of the catalytic base. The structure shows a symmetrical dimer in which two ATP molecules are each sandwiched between the Walker A motif in one subunit and the LSGGQ signature motif in the other subunit. These results establish the stereochemical basis of the power stroke of ABC transporter pumps. | ||
==About this Structure== | ==About this Structure== | ||
1L2T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with NA, ATP and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1L2T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2T OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hunt, J | [[Category: Hunt, J F.]] | ||
[[Category: Karpowich, N.]] | [[Category: Karpowich, N.]] | ||
[[Category: Rosen, J.]] | [[Category: Rosen, J.]] | ||
[[Category: Smith, P | [[Category: Smith, P C.]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: IPA]] | [[Category: IPA]] | ||
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[[Category: walker-a]] | [[Category: walker-a]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:40 2008'' | ||
Revision as of 14:40, 21 February 2008
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Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette
OverviewOverview
It has been proposed that the reaction cycle of ATP binding cassette (ABC) transporters is driven by dimerization of their ABC motor domains upon binding ATP at their mutual interface. However, no such ATP sandwich complex has been observed for an ABC from an ABC transporter. In this paper, we report the crystal structure of a stable dimer formed by the E171Q mutant of the MJ0796 ABC, which is hydrolytically inactive due to mutation of the catalytic base. The structure shows a symmetrical dimer in which two ATP molecules are each sandwiched between the Walker A motif in one subunit and the LSGGQ signature motif in the other subunit. These results establish the stereochemical basis of the power stroke of ABC transporter pumps.
About this StructureAbout this Structure
1L2T is a Single protein structure of sequence from Methanocaldococcus jannaschii with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer., Smith PC, Karpowich N, Millen L, Moody JE, Rosen J, Thomas PJ, Hunt JF, Mol Cell. 2002 Jul;10(1):139-49. PMID:12150914
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