1q12
From Proteopedia
(New page: 200px<br /><applet load="1q12" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q12, resolution 2.60Å" /> '''Crystal Structure of...) |
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| - | [[Image:1q12.gif|left|200px]]<br /><applet load="1q12" size=" | + | [[Image:1q12.gif|left|200px]]<br /><applet load="1q12" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q12, resolution 2.60Å" /> | caption="1q12, resolution 2.60Å" /> | ||
'''Crystal Structure of the ATP-bound E. coli MalK'''<br /> | '''Crystal Structure of the ATP-bound E. coli MalK'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ATPase components of ATP binding cassette (ABC) transporters power the | + | The ATPase components of ATP binding cassette (ABC) transporters power the transporters by binding and hydrolyzing ATP. Major conformational changes of an ATPase are revealed by crystal structures of MalK, the ATPase subunit of the maltose transporter from Escherichia coli, in three different dimeric configurations. While other nucleotide binding domains or subunits display low affinity for each other in the absence of the transmembrane segments, the MalK dimer is stabilized through interactions of the additional C-terminal domains. In the two nucleotide-free structures, the N-terminal nucleotide binding domains are separated to differing degrees, and the dimer is maintained through contacts of the C-terminal regulatory domains. In the ATP-bound form, the nucleotide binding domains make contact and two ATPs lie buried along the dimer interface. The two nucleotide binding domains of the dimer open and close like a pair of tweezers, suggesting a regulatory mechanism for ATPase activity that may be tightly coupled to translocation. |
==About this Structure== | ==About this Structure== | ||
| - | 1Q12 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 ATP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1Q12 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=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q12 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, J.]] | [[Category: Chen, J.]] | ||
| - | [[Category: Davidson, A | + | [[Category: Davidson, A L.]] |
[[Category: Lin, J.]] | [[Category: Lin, J.]] | ||
[[Category: Lu, G.]] | [[Category: Lu, G.]] | ||
| - | [[Category: Quiocho, F | + | [[Category: Quiocho, F A.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: atp-binding cassette]] | [[Category: atp-binding cassette]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:44 2008'' |
Revision as of 12:34, 21 February 2008
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Crystal Structure of the ATP-bound E. coli MalK
Overview
The ATPase components of ATP binding cassette (ABC) transporters power the transporters by binding and hydrolyzing ATP. Major conformational changes of an ATPase are revealed by crystal structures of MalK, the ATPase subunit of the maltose transporter from Escherichia coli, in three different dimeric configurations. While other nucleotide binding domains or subunits display low affinity for each other in the absence of the transmembrane segments, the MalK dimer is stabilized through interactions of the additional C-terminal domains. In the two nucleotide-free structures, the N-terminal nucleotide binding domains are separated to differing degrees, and the dimer is maintained through contacts of the C-terminal regulatory domains. In the ATP-bound form, the nucleotide binding domains make contact and two ATPs lie buried along the dimer interface. The two nucleotide binding domains of the dimer open and close like a pair of tweezers, suggesting a regulatory mechanism for ATPase activity that may be tightly coupled to translocation.
About this Structure
1Q12 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle., Chen J, Lu G, Lin J, Davidson AL, Quiocho FA, Mol Cell. 2003 Sep;12(3):651-61. PMID:14527411
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