1l2t: Difference between revisions

Revision as of 11:34, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1l2t.png

Template:STRUCTURE 1l2t

Dimeric Structure of MJ0796, a Bacterial ABC Transporter CassetteDimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette

Template:ABSTRACT PUBMED 12150914

About this StructureAbout this Structure

1L2T is a Single protein structure of sequence from Methanocaldococcus jannaschii. 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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OCA

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-'''Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette'''
+===Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12150914}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12150914}}
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 [[Category: Nbd]]
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