2awo

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(New page: 200px<br /><applet load="2awo" size="450" color="white" frame="true" align="right" spinBox="true" caption="2awo, resolution 2.80&Aring;" /> '''Crystal structure of...)
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[[Image:2awo.gif|left|200px]]<br /><applet load="2awo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2awo, resolution 2.80&Aring;" />
 
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'''Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ADP-Mg)'''<br />
 
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==Overview==
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==Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ADP-Mg)==
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ATP-binding cassette (ABC) transporters couple ATP binding and hydrolysis, to the movement of substances across the membrane; conformational changes, clearly play an important role in the transporter mechanism. Previously, we have shown that a dimer of MalK, the ATPase subunit of the maltose, transporter from Escherichia coli, undergoes a tweezers-like motion in a, transport cycle. The MalK monomer consists of an N-terminal nucleotide, binding domain and a C-terminal regulatory domain. The two, nucleotide-binding domains in a dimer are either open or closed, depending, on whether ATP is present, while the regulatory domains maintain contacts, to hold the dimer together. In this work, the structure of MalK in a, posthydrolysis state is presented, obtained by cocrystallizing MalK with, ATP-Mg(2+). ATP was hydrolyzed in the crystallization drop, and ADP-Mg(2+), was found in the resulting crystal structure. In contrast to the ATP-bound, form where two ATP molecules are buried in a closed interface between the, nucleotide-binding domains, the two nucleotide-binding domains of the, ADP-bound form are open, indicating that ADP, unlike ATP, cannot stabilize, the closed form. This conclusion is further supported by oligomerization, studies of MalK in solution. At low protein concentrations, ATP promotes, dimerization of MalK, whereas ADP does not. The structures of dimeric MalK, in the nucleotide-free, ATP-bound, and ADP-bound forms provide a framework, for understanding the nature of the conformational changes that occur in, an ATP-binding cassette transporter hydrolysis cycle, as well as how, conformational changes in MalK are coupled to solute transport.
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<StructureSection load='2awo' size='340' side='right'caption='[[2awo]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2awo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AWO FirstGlance]. <br>
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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]] 2.8&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2awo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2awo OCA], [https://pdbe.org/2awo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2awo RCSB], [https://www.ebi.ac.uk/pdbsum/2awo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2awo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MALK_ECOLI MALK_ECOLI] Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/2awo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2awo ConSurf].
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<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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ATP-binding cassette (ABC) transporters couple ATP binding and hydrolysis to the movement of substances across the membrane; conformational changes clearly play an important role in the transporter mechanism. Previously, we have shown that a dimer of MalK, the ATPase subunit of the maltose transporter from Escherichia coli, undergoes a tweezers-like motion in a transport cycle. The MalK monomer consists of an N-terminal nucleotide binding domain and a C-terminal regulatory domain. The two nucleotide-binding domains in a dimer are either open or closed, depending on whether ATP is present, while the regulatory domains maintain contacts to hold the dimer together. In this work, the structure of MalK in a posthydrolysis state is presented, obtained by cocrystallizing MalK with ATP-Mg(2+). ATP was hydrolyzed in the crystallization drop, and ADP-Mg(2+) was found in the resulting crystal structure. In contrast to the ATP-bound form where two ATP molecules are buried in a closed interface between the nucleotide-binding domains, the two nucleotide-binding domains of the ADP-bound form are open, indicating that ADP, unlike ATP, cannot stabilize the closed form. This conclusion is further supported by oligomerization studies of MalK in solution. At low protein concentrations, ATP promotes dimerization of MalK, whereas ADP does not. The structures of dimeric MalK in the nucleotide-free, ATP-bound, and ADP-bound forms provide a framework for understanding the nature of the conformational changes that occur in an ATP-binding cassette transporter hydrolysis cycle, as well as how conformational changes in MalK are coupled to solute transport.
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==About this Structure==
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ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation.,Lu G, Westbrooks JM, Davidson AL, Chen J Proc Natl Acad Sci U S A. 2005 Dec 13;102(50):17969-74. Epub 2005 Dec 2. PMID:16326809<ref>PMID:16326809</ref>
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2AWO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Maltose-transporting_ATPase Maltose-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.19 3.6.3.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AWO OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation., Lu G, Westbrooks JM, Davidson AL, Chen J, Proc Natl Acad Sci U S A. 2005 Dec 13;102(50):17969-74. Epub 2005 Dec 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16326809 16326809]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2awo" style="background-color:#fffaf0;"></div>
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[[Category: Maltose-transporting ATPase]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Chen, J.]]
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__TOC__
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[[Category: Davidson, A.L.]]
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</StructureSection>
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[[Category: Lu, G.]]
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[[Category: Escherichia coli K-12]]
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[[Category: Westbrooks, J.M.]]
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[[Category: Large Structures]]
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[[Category: ADP]]
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[[Category: Chen J]]
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[[Category: MG]]
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[[Category: Davidson AL]]
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[[Category: atp-binding cassette]]
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[[Category: Lu G]]
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[[Category: Westbrooks JM]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:25:35 2007''
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Current revision

Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ADP-Mg)

PDB ID 2awo

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