View source for 5dbl


==Crystal structure of the Staphylococcus aureus SasG E1-G52 Y625W mutant==
<StructureSection load='5dbl' size='340' side='right'caption='[[5dbl]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dbl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DBL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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=5dbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dbl OCA], [https://pdbe.org/5dbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dbl RCSB], [https://www.ebi.ac.uk/pdbsum/5dbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dbl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SASG_STAA8 SASG_STAA8] Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non-differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation.<ref>PMID:14523109</ref> <ref>PMID:17660408</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many human proteins contain intrinsically disordered regions, and disorder in these proteins can be fundamental to their function-for example, facilitating transient but specific binding, promoting allostery, or allowing efficient posttranslational modification. SasG, a multidomain protein implicated in host colonization and biofilm formation in Staphylococcus aureus, provides another example of how disorder can play an important role. Approximately one-half of the domains in the extracellular repetitive region of SasG are intrinsically unfolded in isolation, but these E domains fold in the context of their neighboring folded G5 domains. We have previously shown that the intrinsic disorder of the E domains mediates long-range cooperativity between nonneighboring G5 domains, allowing SasG to form a long, rod-like, mechanically strong structure. Here, we show that the disorder of the E domains coupled with the remarkable stability of the interdomain interface result in cooperative folding kinetics across long distances. Formation of a small structural nucleus at one end of the molecule results in rapid structure formation over a distance of 10 nm, which is likely to be important for the maintenance of the structural integrity of SasG. Moreover, if this normal folding nucleus is disrupted by mutation, the interdomain interface is sufficiently stable to drive the folding of adjacent E and G5 domains along a parallel folding pathway, thus maintaining cooperative folding.

Disorder drives cooperative folding in a multidomain protein.,Gruszka DT, Mendonca CA, Paci E, Whelan F, Hawkhead J, Potts JR, Clarke J Proc Natl Acad Sci U S A. 2016 Oct 3. pii: 201608762. PMID:27698144<ref>PMID:27698144</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dbl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
[[Category: Potts JR]]
[[Category: Whelan F]]