View source for 4rmb


==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]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rmb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_NEM316 Streptococcus agalactiae NEM316]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4RMB 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]] 1.7&#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=4rmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rmb OCA], [https://pdbe.org/4rmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rmb RCSB], [https://www.ebi.ac.uk/pdbsum/4rmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rmb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8E473_STRA3 Q8E473_STRA3] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rmb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus agalactiae NEM316]]
[[Category: Ponnuraj K]]
[[Category: Sundaresan R]]