1g29
From Proteopedia
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|PDB= 1g29 |SIZE=350|CAPTION= <scene name='initialview01'>1g29</scene>, resolution 1.90Å | |PDB= 1g29 |SIZE=350|CAPTION= <scene name='initialview01'>1g29</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MALK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2265 Thermococcus litoralis]) | |GENE= MALK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2265 Thermococcus litoralis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g29 OCA], [http://www.ebi.ac.uk/pdbsum/1g29 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g29 RCSB]</span> | ||
}} | }} | ||
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[[Category: Vonrhein, C.]] | [[Category: Vonrhein, C.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: DIO]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: NH4]] | ||
| - | [[Category: POP]] | ||
[[Category: active transport]] | [[Category: active transport]] | ||
[[Category: atpase]] | [[Category: atpase]] | ||
[[Category: maltose uptake and regulation]] | [[Category: maltose uptake and regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:35:13 2008'' |
Revision as of 17:35, 30 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Gene: | MALK (Thermococcus litoralis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 20:35:13 2008
