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| | <StructureSection load='5tu8' size='340' side='right'caption='[[5tu8]], [[Resolution|resolution]] 2.33Å' scene=''> | | <StructureSection load='5tu8' size='340' side='right'caption='[[5tu8]], [[Resolution|resolution]] 2.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tu8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staeq Staeq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TU8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tu8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis_RP62A Staphylococcus epidermidis RP62A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TU8 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tu7|5tu7]], [[5tu9|5tu9]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aap, SERP2398 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=176279 STAEQ])</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=5tu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tu8 OCA], [https://pdbe.org/5tu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tu8 RCSB], [https://www.ebi.ac.uk/pdbsum/5tu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tu8 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=5tu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tu8 OCA], [http://pdbe.org/5tu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tu8 RCSB], [http://www.ebi.ac.uk/pdbsum/5tu8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tu8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5HKE8_STAEQ Q5HKE8_STAEQ] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Staeq]] | + | [[Category: Staphylococcus epidermidis RP62A]] |
| - | [[Category: Conrady, D G]] | + | [[Category: Conrady DG]] |
| - | [[Category: Herr, A B]] | + | [[Category: Herr AB]] |
| - | [[Category: Shelton, C L]] | + | [[Category: Shelton CL]] |
| - | [[Category: Biofilm intercellular adhesion staphylococcus aap]]
| + | |
| - | [[Category: Protein binding]]
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| Structural highlights
Function
Q5HKE8_STAEQ
Publication Abstract from PubMed
Staphylococcus epidermidis is an opportunistic pathogen that can form robust biofilms that render the bacteria resistant to antibiotic action and immune responses. Intercellular adhesion in S. epidermidis biofilms is mediated by the cell wall-associated Accumulation-Associated Protein (Aap), via zinc-mediated self-assembly of its B-repeat region. This region contains up to 17 nearly-identical sequence repeats, with each repeat assumed to be functionally equivalent. However, Aap B-repeats exist as two subtypes, defined by a cluster of consensus or variant amino acids. These variable residues are positioned near the zinc-binding (and dimerization) site and the stability determinant for the B-repeat fold. We have characterized four B-repeat constructs to assess the functional relevance of the two Aap B-repeat subtypes. Analytical ultracentrifugation experiments demonstrated that constructs with the variant sequence show reduced or absent Zn2+-induced dimerization. Likewise, circular dichroism thermal denaturation experiments showed that the variant sequence could significantly stabilize the fold, depending on its location within the construct. Crystal structures of three of the constructs revealed that the side chains from the variant sequence form an extensive bonding network that can stabilize the fold. Furthermore, altered distribution of charged residues between consensus and variant sequences changes the electrostatic potential in the vicinity of the Zn2+ binding site, providing a mechanistic explanation for the loss of zinc-induced dimerization in the variant constructs. These data suggest an assembly code that defines preferred oligomerization modes of the B-repeat region of Aap and a slip-grip model for initial contact and firm intercellular adhesion during biofilm formation.
Functional consequences of B-repeat sequence variation in the Staphylococcal biofilm protein Aap: Deciphering the assembly code.,Shelton CL, Conrady DG, Herr AB Biochem J. 2016 Nov 21. pii: BCJ20160675. PMID:27872164[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shelton CL, Conrady DG, Herr AB. Functional consequences of B-repeat sequence variation in the Staphylococcal biofilm protein Aap: Deciphering the assembly code. Biochem J. 2016 Nov 21. pii: BCJ20160675. PMID:27872164 doi:http://dx.doi.org/10.1042/BCJ20160675
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