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J. Biol. Chem., Vol. 276, Issue 34, 32313-32321, August 24, 2001
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From the The crystal structure of the MJ0796
ATP-binding cassette, a member of the o228/LolD transporter family, has
been determined at 2.7-Å resolution with MgADP bound at its active
site. Comparing this structure with that of the ATP-bound form of the
HisP ATP-binding cassette (Hung, L. W., Wang, I. X.,
Nikaido, K., Liu, P. Q., Ames, G. F., and Kim, S. H. (1998) Nature 396, 703-707) shows a 5-Å withdrawal of a
phylogenetically invariant glutamine residue from contact with the
The atomic coordinates and the structure factors (code 1F30) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
The Crystal Structure of the MJ0796 ATP-binding
Cassette
IMPLICATIONS FOR THE STRUCTURAL CONSEQUENCES OF ATP HYDROLYSIS
IN THE ACTIVE SITE OF AN ABC TRANSPORTER*
,,,
Department of Biological Sciences, Columbia
University, New York, New York 10027 and the § Department of
Physiology, University of Texas Southwestern Medical Center,
Dallas, Texas 75235-9040
-phosphate of ATP in the active site. This glutamine is located in a
protein segment that links the rigid F1-type ATP-binding core of the enzyme to an ABC transporter-specific 
-helical subdomain that moves substantially away from the active site in the MgADP-bound structure of MJ0796 compared with the ATP-bound structure of HisP. A
similar conformational effect is observed in the MgADP-bound structure
of MJ1267 (Karpowich, N., et al. (2001)
Structure, in press), establishing the withdrawal of the
glutamine and the coupled outward rotation of the -helical subdomain
as consistent consequences of -phosphate release from the active
site of the transporter. Considering this subdomain movement in the
context of a leading model for the physiological dimer of cassettes
present in ABC transporters indicates that it produces a modest
mechanical change that is likely to play a role in facilitating
nucleotide exchange out of the ATPase active site. Finally, it is
noteworthy that one of the intersubunit packing interactions in the
MJ0796 crystal involves antiparallel 
-type hydrogen bonding
interactions between the outermost -strands in the two core
-sheets, leading to their fusion into a single extended -sheet, a
type of structural interaction that has been proposed to play a role in
mediating the aggregation of -sheet-containing proteins.
*
This work was supported by a start-up grant from Columbia
University, a Basil O'Connor starter scholar award from the March of
Dimes, and a research grant from the Cystic Fibrosis Foundation (to
J. F.H.) and by grants from the National Institutes of Health and the
Welch Foundation (to P. J. T.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Biological Sciences, 702A Fairchild Center, MC2434, Columbia
University, New York, NY 10027. Tel.: 212-854-5443; Fax: 212-865-8246;
E-mail: hunt@sid.bio.columbia.edu.
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