1g29
From Proteopedia
(New page: 200px<br /><applet load="1g29" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g29, resolution 1.90Å" /> '''MALK'''<br /> ==Ove...) |
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| - | [[Image:1g29.jpg|left|200px]]<br /><applet load="1g29" size=" | + | [[Image:1g29.jpg|left|200px]]<br /><applet load="1g29" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g29, resolution 1.90Å" /> | caption="1g29, resolution 1.90Å" /> | ||
'''MALK'''<br /> | '''MALK'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The members of the ABC transporter family transport a wide variety of | + | The members of the ABC transporter family transport a wide variety of molecules into or out of cells and cellular compartments. Apart from a translocation pore, each member possesses two similar nucleoside triphosphate-binding subunits or domains in order to couple the energy-providing reaction with transport. In the maltose transporter of several Gram-negative bacteria and the archaeon Thermo coccus litoralis, the nucleoside triphosphate-binding subunit contains a C-terminal regulatory domain. A dimer of the subunit is attached cytoplasmically to the translocation pore. Here we report the crystal structure of this dimer showing two bound pyrophosphate molecules at 1.9 A resolution. The dimer forms by association of the ATPase domains, with the two regulatory domains attached at opposite poles. Significant deviation from 2-fold symmetry is seen at the interface of the dimer and in the regions corresponding to those residues known to be in contact with the translocation pore. The structure and its relationship to function are discussed in the light of known mutations from the homologous Escherichia coli and Salmonella typhimurium proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1G29 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis] with NH4, MG, CL, NA, POP and DIO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1G29 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis] with <scene name='pdbligand=NH4:'>NH4</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=POP:'>POP</scene> and <scene name='pdbligand=DIO:'>DIO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G29 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: maltose uptake and regulation]] | [[Category: maltose uptake and regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:16 2008'' |
Revision as of 10:45, 21 February 2008
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MALK
Overview
The members of the ABC transporter family transport a wide variety of molecules into or out of cells and cellular compartments. Apart from a translocation pore, each member possesses two similar nucleoside triphosphate-binding subunits or domains in order to couple the energy-providing reaction with transport. In the maltose transporter of several Gram-negative bacteria and the archaeon Thermo coccus litoralis, the nucleoside triphosphate-binding subunit contains a C-terminal regulatory domain. A dimer of the subunit is attached cytoplasmically to the translocation pore. Here we report the crystal structure of this dimer showing two bound pyrophosphate molecules at 1.9 A resolution. The dimer forms by association of the ATPase domains, with the two regulatory domains attached at opposite poles. Significant deviation from 2-fold symmetry is seen at the interface of the dimer and in the regions corresponding to those residues known to be in contact with the translocation pore. The structure and its relationship to function are discussed in the light of known mutations from the homologous Escherichia coli and Salmonella typhimurium proteins.
About this Structure
1G29 is a Single protein structure of sequence from Thermococcus litoralis with , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis., Diederichs K, Diez J, Greller G, Muller C, Breed J, Schnell C, Vonrhein C, Boos W, Welte W, EMBO J. 2000 Nov 15;19(22):5951-61. PMID:11080142
Page seeded by OCA on Thu Feb 21 12:45:16 2008
Categories: Single protein | Thermococcus litoralis | Boos, W. | Breed, J. | Diederichs, K. | Diez, J. | Greller, G. | Mueller, C. | Schnell, C. | Vonrhein, C. | Welte, W. | CL | DIO | MG | NA | NH4 | POP | Active transport | Atpase | Maltose uptake and regulation
