7avh

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Current revision (07:45, 1 May 2024) (edit) (undo)
 
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<StructureSection load='7avh' size='340' side='right'caption='[[7avh]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
<StructureSection load='7avh' size='340' side='right'caption='[[7avh]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7avh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strgc Strgc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AVH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7avh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_gordonii_str._Challis_substr._CH1 Streptococcus gordonii str. Challis substr. CH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AVH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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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]] 1.35&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5lrh|5lrh]]</div></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SGO_0707 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=467705 STRGC])</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=7avh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7avh OCA], [https://pdbe.org/7avh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7avh RCSB], [https://www.ebi.ac.uk/pdbsum/7avh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7avh 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=7avh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7avh OCA], [https://pdbe.org/7avh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7avh RCSB], [https://www.ebi.ac.uk/pdbsum/7avh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7avh ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A8AW49_STRGC A8AW49_STRGC]
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Changes at the cell surface enable bacteria to survive in dynamic environments, such as diverse niches of the human host. Here, we reveal "Periscope Proteins" as a widespread mechanism of bacterial surface alteration mediated through protein length variation. Tandem arrays of highly similar folded domains can form an elongated rod-like structure; thus, variation in the number of domains determines how far an N-terminal host ligand binding domain projects from the cell surface. Supported by newly available long-read genome sequencing data, we propose that this class could contain over 50 distinct proteins, including those implicated in host colonization and biofilm formation by human pathogens. In large multidomain proteins, sequence divergence between adjacent domains appears to reduce interdomain misfolding. Periscope Proteins break this "rule," suggesting that their length variability plays an important role in regulating bacterial interactions with host surfaces, other bacteria, and the immune system.
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Periscope Proteins are variable-length regulators of bacterial cell surface interactions.,Whelan F, Lafita A, Gilburt J, Degut C, Griffiths SC, Jenkins HT, St John AN, Paci E, Moir JWB, Plevin MJ, Baumann CG, Bateman A, Potts JR Proc Natl Acad Sci U S A. 2021 Jun 8;118(23). pii: 2101349118. doi:, 10.1073/pnas.2101349118. PMID:34074781<ref>PMID:34074781</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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<div class="pdbe-citations 7avh" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Strgc]]
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[[Category: Streptococcus gordonii str. Challis substr. CH1]]
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[[Category: Jenkins, H T]]
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[[Category: Jenkins HT]]
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[[Category: Potts, J R]]
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[[Category: Potts JR]]
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[[Category: Whelan, F]]
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[[Category: Whelan F]]
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[[Category: Adhesin]]
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[[Category: Bacterial surface]]
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[[Category: Cell adhesion]]
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[[Category: Sgo0707]]
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[[Category: Tandem repeat]]
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Current revision

Streptococcal High Identity Repeats in Tandem (SHIRT) domains 3-4 from cell surface protein SGO_0707

PDB ID 7avh

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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