2ixf

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[[Image:2ixf.png|left|200px]]
 
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==Crystal structure of the ATPase domain of TAP1 with ATP (D645Q, Q678H mutant)==
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The line below this paragraph, containing "STRUCTURE_2ixf", creates the "Structure Box" on the page.
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<StructureSection load='2ixf' size='340' side='right'caption='[[2ixf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ixf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IXF 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&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_2ixf| PDB=2ixf | SCENE= }}
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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=2ixf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixf OCA], [https://pdbe.org/2ixf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ixf RCSB], [https://www.ebi.ac.uk/pdbsum/2ixf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ixf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TAP1_RAT TAP1_RAT] Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin (By similarity).
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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/ix/2ixf_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=2ixf 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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The ABC transporter associated with antigen processing (TAP) shuttles cytosolic peptides into the endoplasmic reticulum for loading onto class I MHC molecules. Transport is fueled by ATP binding and hydrolysis at two distinct cytosolic ATPase sites. One site comprises consensus motifs shared among most ABC transporters, while the second has substituted, degenerate motifs. Biochemical and crystallography experiments with a TAP cytosolic domain demonstrate that the consensus ATPase site has high catalytic activity and facilitates ATP-dependent dimerization of the cytosolic domains, which is an important conformational change during transport. In contrast, the degenerate site is defective in dimerization and ATP hydrolysis. Full-length TAP mutagenesis demonstrates the necessity for at least one consensus site, supporting our conclusion that the consensus site is the principal facilitator of substrate transport. Since asymmetry of the ATPase site motifs is a feature of many mammalian homologs, our proposed model has broad implications for ABC transporters.
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===CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645Q, Q678H MUTANT)===
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Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter.,Procko E, Ferrin-O'Connell I, Ng SL, Gaudet R Mol Cell. 2006 Oct 6;24(1):51-62. PMID:17018292<ref>PMID:17018292</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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The line below this paragraph, {{ABSTRACT_PUBMED_17018292}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2ixf" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17018292 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17018292}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[2ixf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXF OCA].
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==Reference==
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<ref group="xtra">PMID:017018292</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Connell, I Ferrin-O.]]
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[[Category: Ferrin-O'Connell I]]
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[[Category: Gaudet, R.]]
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[[Category: Gaudet R]]
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[[Category: Ng, S L.]]
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[[Category: Ng S-L]]
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[[Category: Procko, E.]]
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[[Category: Procko E]]
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[[Category: Abc protein transport]]
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[[Category: Hydrolase]]
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[[Category: Membrane]]
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[[Category: Nucleotide-binding]]
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[[Category: Transport]]
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Current revision

Crystal structure of the ATPase domain of TAP1 with ATP (D645Q, Q678H mutant)

PDB ID 2ixf

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