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1f3o

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(New page: 200px<br /><applet load="1f3o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f3o, resolution 2.70&Aring;" /> '''Crystal structure of...)
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[[Image:1f3o.gif|left|200px]]<br /><applet load="1f3o" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1f3o, resolution 2.70&Aring;" />
 
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'''Crystal structure of MJ0796 ATP-binding cassette'''<br />
 
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==Overview==
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==Crystal structure of MJ0796 ATP-binding cassette==
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The crystal structure of the MJ0796 ATP-binding cassette, a member of the, o228/LolD transporter family, has been determined at 2.7-A resolution with, MgADP bound at its active site. Comparing this structure with that of the, ATP-bound form of the HisP ATP-binding cassette (Hung, L. W., Wang, I. X., Nikaido, K., Liu, P. Q., Ames, G. F., and Kim, S. H. (1998) Nature 396, 703-707) shows a 5-A withdrawal of a phylogenetically invariant glutamine, residue from contact with the gamma-phosphate of ATP in the active site., This glutamine is located in a protein segment that links the rigid, F(1)-type ATP-binding core of the enzyme to an ABC transporter-specific, alpha-helical subdomain that moves substantially away from the active site, in the MgADP-bound structure of MJ0796 compared with the ATP-bound, structure of HisP. A similar conformational effect is observed in the, MgADP-bound structure of MJ1267 (Karpowich, N., et al. (2001) Structure, in press), establishing the withdrawal of the glutamine and the coupled, outward rotation of the alpha-helical subdomain as consistent consequences, of gamma-phosphate release from the active site of the transporter., Considering this subdomain movement in the context of a leading model for, the physiological dimer of cassettes present in ABC transporters indicates, that it produces a modest mechanical change that is likely to play a role, in facilitating nucleotide exchange out of the ATPase active site., Finally, it is noteworthy that one of the intersubunit packing, interactions in the MJ0796 crystal involves antiparallel beta-type, hydrogen bonding interactions between the outermost beta-strands in the, two core beta-sheets, leading to their fusion into a single extended, beta-sheet, a type of structural interaction that has been proposed to, play a role in mediating the aggregation of beta-sheet-containing, proteins.
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<StructureSection load='1f3o' size='340' side='right'caption='[[1f3o]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1f3o]] is a 1 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=1F3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3O FirstGlance]. <br>
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1F3O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F3O OCA].
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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]] 2.7&#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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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==Reference==
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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=1f3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3o OCA], [https://pdbe.org/1f3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3o RCSB], [https://www.ebi.ac.uk/pdbsum/1f3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3o ProSAT]</span></td></tr>
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The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter., Yuan YR, Blecker S, Martsinkevich O, Millen L, Thomas PJ, Hunt JF, J Biol Chem. 2001 Aug 24;276(34):32313-21. Epub 2001 Jun 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11402022 11402022]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Y796_METJA Y796_METJA]
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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/f3/1f3o_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=1f3o ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
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[[Category: Single protein]]
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[[Category: Hunt JF]]
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[[Category: Hunt, J.F.]]
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[[Category: Yuan Y-R]]
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[[Category: Yuan, Y.R.]]
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[[Category: ADP]]
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[[Category: MG]]
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[[Category: transporter]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:35:05 2007''
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Current revision

Crystal structure of MJ0796 ATP-binding cassette

PDB ID 1f3o

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