5mkk: Difference between revisions
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<StructureSection load='5mkk' size='340' side='right' caption='[[5mkk]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='5mkk' size='340' side='right' caption='[[5mkk]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5mkk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MKK FirstGlance]. <br> | <table><tr><td colspan='2'>[[5mkk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MKK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TT_C0976 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2]), TT_C0977 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</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=5mkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkk OCA], [http://pdbe.org/5mkk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mkk RCSB], [http://www.ebi.ac.uk/pdbsum/5mkk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkk ProSAT]</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=5mkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkk OCA], [http://pdbe.org/5mkk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mkk RCSB], [http://www.ebi.ac.uk/pdbsum/5mkk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Thet2]] | |||
[[Category: Diederichs, K]] | [[Category: Diederichs, K]] | ||
[[Category: Noell, A]] | [[Category: Noell, A]] | ||
Revision as of 09:57, 31 January 2018
Crystal structure of the heterodimeric ABC transporter TmrAB, a homolog of the antigen translocation complex TAPCrystal structure of the heterodimeric ABC transporter TmrAB, a homolog of the antigen translocation complex TAP
Structural highlights
Publication Abstract from PubMedABC transporters form one of the largest protein superfamilies in all domains of life, catalyzing the movement of diverse substrates across membranes. In this key position, ABC transporters can mediate multidrug resistance in cancer therapy and their dysfunction is linked to various diseases. Here, we describe the 2.7-A X-ray structure of heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), which not only shares structural homology with the antigen translocation complex TAP, but is also able to restore antigen processing in human TAP-deficient cells. TmrAB exhibits a broad peptide specificity and can concentrate substrates several thousandfold, using only one single active ATP-binding site. In our structure, TmrAB adopts an asymmetric inward-facing state, and we show that the C-terminal helices, arranged in a zipper-like fashion, play a crucial role in guiding the conformational changes associated with substrate transport. In conclusion, TmrAB can be regarded as a model system for asymmetric ABC exporters in general, and for TAP in particular. Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP.,Noll A, Thomas C, Herbring V, Zollmann T, Barth K, Mehdipour AR, Tomasiak TM, Bruchert S, Joseph B, Abele R, Olieric V, Wang M, Diederichs K, Hummer G, Stroud RM, Pos KM, Tampe R Proc Natl Acad Sci U S A. 2017 Jan 9. pii: 201620009. doi:, 10.1073/pnas.1620009114. PMID:28069938[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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