1g29

From Proteopedia

(Difference between revisions)

Revision as of 23:34, 10 September 2015

MALK

Structural highlights

1g29 is a 2 chain structure with sequence from 'caldococcus litoralis' z-1301. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Gene:	MALK ('Caldococcus litoralis' Z-1301)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[MALK_THELN] Part of the ABC transporter complex MalEFGK involved in trehalose/maltose import. Responsible for energy coupling to the transport system.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Greller G, Horlacher R, DiRuggiero J, Boos W. Molecular and biochemical analysis of MalK, the ATP-hydrolyzing subunit of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. J Biol Chem. 1999 Jul 16;274(29):20259-64. PMID:10400644
↑ Greller G, Riek R, Boos W. Purification and characterization of the heterologously expressed trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon Thermococcus litoralis. Eur J Biochem. 2001 Jul;268(14):4011-8. PMID:11453995
↑ Xavier KB, Martins LO, Peist R, Kossmann M, Boos W, Santos H. High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis. J Bacteriol. 1996 Aug;178(16):4773-7. PMID:8759837
↑ Diederichs K, Diez J, Greller G, Muller C, Breed J, Schnell C, Vonrhein C, Boos W, Welte W. Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J. 2000 Nov 15;19(22):5951-61. PMID:11080142 doi:10.1093/emboj/19.22.5951

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g29"

@@ Line 2: / Line 2: @@
 <StructureSection load='1g29' size='340' side='right' caption='[[1g29]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1g29]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G29 FirstGlance]. <br>
+<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G29 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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 Thermococcus litoralis])</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://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.rcsb.org/pdb/explore.do?structureId=1g29 RCSB], [http://www.ebi.ac.uk/pdbsum/1g29 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1g29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g29 RCSB], [http://www.ebi.ac.uk/pdbsum/1g29 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q9YGA6_THELI Q9YGA6_THELI]] 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:8759837</ref> <ref>PMID:11453995</ref>
+[[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1g29" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Thermococcus litoralis]]
+[[Category: Caldococcus litoralis z-1301]]
 [[Category: Boos, W]]
 [[Category: Breed, J]]

1g29

From Proteopedia

Revision as of 23:34, 10 September 2015

MALK

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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