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| - | {{Large structure}}
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| | ==Solid-state NMR structure of the membrane anchor domain of the trimeric autotransporter YadA== | | ==Solid-state NMR structure of the membrane anchor domain of the trimeric autotransporter YadA== |
| - | <StructureSection load='2lme' size='340' side='right' caption='[[2lme]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lme' size='340' side='right'caption='[[2lme]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lme]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Yere8 Yere8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LME FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lme]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_enterocolitica_subsp._enterocolitica_8081 Yersinia enterocolitica subsp. enterocolitica 8081]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LME FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yadA, YEP0066 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=393305 YERE8])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=2lme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lme OCA], [http://pdbe.org/2lme PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lme RCSB], [http://www.ebi.ac.uk/pdbsum/2lme PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lme 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=2lme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lme OCA], [https://pdbe.org/2lme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lme RCSB], [https://www.ebi.ac.uk/pdbsum/2lme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lme ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | {{Large structure}} | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YADA_YERE8 YADA_YERE8]] Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes initial attachment and invasion of eukaryotic cells. Also protects the bacteria by being responsible for agglutination, serum resistance, complement inactivation and phagocytosis resistance (By similarity). | + | [https://www.uniprot.org/uniprot/YADA_YERE8 YADA_YERE8] Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes initial attachment and invasion of eukaryotic cells. Also protects the bacteria by being responsible for agglutination, serum resistance, complement inactivation and phagocytosis resistance (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Adhesin|Adhesin]] | + | *[[Adhesin 3D structures|Adhesin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Yere8]] | + | [[Category: Large Structures]] |
| - | [[Category: Bardiaux, B]] | + | [[Category: Yersinia enterocolitica subsp. enterocolitica 8081]] |
| - | [[Category: Franks, W T]] | + | [[Category: Bardiaux B]] |
| - | [[Category: Habeck, M]] | + | [[Category: Franks WT]] |
| - | [[Category: Linke, D]] | + | [[Category: Habeck M]] |
| - | [[Category: Rossum, B van]]
| + | [[Category: Linke D]] |
| - | [[Category: Shahid, S A]] | + | [[Category: Shahid SA]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Van Rossum B]] |
| - | [[Category: Membrane protein]]
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| - | [[Category: Trimeric autotransporter]]
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| Structural highlights
Function
YADA_YERE8 Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes initial attachment and invasion of eukaryotic cells. Also protects the bacteria by being responsible for agglutination, serum resistance, complement inactivation and phagocytosis resistance (By similarity).
Publication Abstract from PubMed
Membrane proteins are largely underrepresented among available atomic-resolution structures. The use of detergents in protein purification procedures hinders the formation of well-ordered crystals for X-ray crystallography and leads to slower molecular tumbling, impeding the application of solution-state NMR. Solid-state magic-angle spinning NMR spectroscopy is an emerging method for membrane-protein structural biology that can overcome these technical problems. Here we present the solid-state NMR structure of the transmembrane domain of the Yersinia enterocolitica adhesin A (YadA). The sample was derived from crystallization trials that yielded only poorly diffracting microcrystals. We solved the structure using a single, uniformly (13)C- and (15)N-labeled sample. In addition, solid-state NMR allowed us to acquire information on the flexibility and mobility of parts of the structure, which, in combination with evolutionary conservation information, presents new insights into the autotransport mechanism of YadA.
Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals.,Shahid SA, Bardiaux B, Franks WT, Krabben L, Habeck M, van Rossum BJ, Linke D Nat Methods. 2012 Dec 7;9(12):1212-7. doi: 10.1038/nmeth.2248. Epub 2012 Nov 11. PMID:23142870[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shahid SA, Bardiaux B, Franks WT, Krabben L, Habeck M, van Rossum BJ, Linke D. Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals. Nat Methods. 2012 Dec 7;9(12):1212-7. doi: 10.1038/nmeth.2248. Epub 2012 Nov 11. PMID:23142870 doi:http://dx.doi.org/10.1038/nmeth.2248
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