1g29

<table><tr><td colspan='2'>[[1g29]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/'caldococcus_litoralis'_z-1301 'caldococcus litoralis' z-1301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G29 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1G29 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MALK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2265 'Caldococcus litoralis' Z-1301])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1g29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g29 OCA], [http://pdbe.org/1g29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g29 RCSB], [http://www.ebi.ac.uk/pdbsum/1g29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g29 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MALK_THELN MALK_THELN]] Part of the ABC transporter complex MalEFGK involved in trehalose/maltose import. Responsible for energy coupling to the transport system.<ref>PMID:10400644</ref> <ref>PMID:11453995</ref> <ref>PMID:8759837</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11080142</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1g29" style="background-color:#fffaf0;"></div>

[[Category: Caldococcus litoralis z-1301]]

[[Category: Boos, W]]

[[Category: Breed, J]]

[[Category: Diederichs, K]]

[[Category: Diez, J]]

[[Category: Greller, G]]

[[Category: Mueller, C]]

[[Category: Schnell, C]]

[[Category: Vonrhein, C]]

[[Category: Welte, W]]

[[Category: Sugar binding protein]]