4rmb: Difference between revisions
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''' | ==Crystal structure of keratin 4 binding domain of surface adhesin Srr-1 of S.agalactiae== | ||
<StructureSection load='4rmb' size='340' side='right' caption='[[4rmb]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4rmb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RMB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RMB FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mbo|4mbo]]</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=4rmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rmb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rmb RCSB], [http://www.ebi.ac.uk/pdbsum/4rmb PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The serine rich repeat protein-1 (Srr-1) is an adhesive protein of Streptococcus agalactiae. It is the first bacterial protein identified to interact with human keratin 4 (K4 or KRT4). Within Srr-1, the residues 311-641 constitute the non-repeat ligand binding region (Srr-1-BR311-641). The C-terminal part of Srr-1-BR311-641, comprising of residues 485-642 (termed Srr-1-K4BD), have been identified to bind to K4. Here we report the crystal structure of recombinant Srr-1-K4BD485-642 and its possible mode of interaction with K4 through docking studies. The dimeric structure of Srr-1-K4BD485-642 reveals a novel two way "slide lock" parallel beta-sheet complementation where the C-terminal strand of one monomer is positioned anti-parallel to the N-terminal strand of the adjacent monomer and this arrangement is not seen so far in any of the homologous structures. The dimerization of Srr-1-K4BD485-642 observed both in the crystal structure and in solution suggests that similar domain association could also be possible in in vivo and we propose this association would likely generate a new binding site for another host molecule. It is likely that the adhesin can recognize multiple ligands using its ligand binding sub-domains through their intra and inter domain association with one another. | |||
Structure of KRT4 binding domain of Srr-1 from Streptococcus agalactiae reveals a novel beta-sheet complementation.,Sundaresan R, Samen U, Ponnuraj K Int J Biol Macromol. 2015 Jan 17;75C:97-105. doi: 10.1016/j.ijbiomac.2014.12.048. PMID:25603146<ref>PMID:25603146</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ponnuraj, K]] | |||
[[Category: Sundaresan, R]] | [[Category: Sundaresan, R]] | ||
[[Category: | [[Category: Adhesin]] | ||
[[Category: Bacterial cell surface]] | |||
[[Category: Beta sheet complementation]] | |||
[[Category: Cell adhesion]] | |||
[[Category: Keratin 4]] | |||
[[Category: Variant of dev-igg fold]] | |||
Revision as of 11:54, 12 February 2015
Crystal structure of keratin 4 binding domain of surface adhesin Srr-1 of S.agalactiae
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