1l2t

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Current revision (07:29, 14 February 2024) (edit) (undo)
 
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<StructureSection load='1l2t' size='340' side='right'caption='[[1l2t]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1l2t' size='340' side='right'caption='[[1l2t]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1l2t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L2T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1l2t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L2T FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2t OCA], [https://pdbe.org/1l2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2t RCSB], [https://www.ebi.ac.uk/pdbsum/1l2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2t ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2t OCA], [https://pdbe.org/1l2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2t RCSB], [https://www.ebi.ac.uk/pdbsum/1l2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2t ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Y796_METJA Y796_METJA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l2t ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l2t ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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It has been proposed that the reaction cycle of ATP binding cassette (ABC) transporters is driven by dimerization of their ABC motor domains upon binding ATP at their mutual interface. However, no such ATP sandwich complex has been observed for an ABC from an ABC transporter. In this paper, we report the crystal structure of a stable dimer formed by the E171Q mutant of the MJ0796 ABC, which is hydrolytically inactive due to mutation of the catalytic base. The structure shows a symmetrical dimer in which two ATP molecules are each sandwiched between the Walker A motif in one subunit and the LSGGQ signature motif in the other subunit. These results establish the stereochemical basis of the power stroke of ABC transporter pumps.
 
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ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer.,Smith PC, Karpowich N, Millen L, Moody JE, Rosen J, Thomas PJ, Hunt JF Mol Cell. 2002 Jul;10(1):139-49. PMID:12150914<ref>PMID:12150914</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1l2t" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43067]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hunt, J F]]
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[[Category: Methanocaldococcus jannaschii]]
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[[Category: Karpowich, N]]
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[[Category: Hunt JF]]
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[[Category: Rosen, J]]
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[[Category: Karpowich N]]
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[[Category: Smith, P C]]
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[[Category: Rosen J]]
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[[Category: Abc transporter]]
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[[Category: Smith PC]]
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[[Category: Atpase]]
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[[Category: Nbd]]
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[[Category: Transport protein]]
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[[Category: Walker-a]]
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Current revision

Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette

PDB ID 1l2t

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