View source for 5lnl


==Crystal structure of Hsf 1608-1749 putative domain 1==
<StructureSection load='5lnl' size='340' side='right'caption='[[5lnl]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lnl]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LNL 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]] 3.3&#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=5lnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lnl OCA], [https://pdbe.org/5lnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lnl RCSB], [https://www.ebi.ac.uk/pdbsum/5lnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lnl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P71401_HAEIF P71401_HAEIF] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Haemophilus surface fibril (Hsf) is an unusually large trimeric autotransporter adhesin (TAA) expressed by the most virulent strains of H. influenzae. Hsf is known to mediate adhesion between pathogen and host, allowing the establishment of potentially deadly diseases such as epiglottitis, meningitis and pneumonia. While recent research has suggested that this TAA might adopt a novel `hairpin-like' architecture, the characterization of Hsf has been limited to in silico modelling and electron micrographs, with no high-resolution structural data available. Here, the crystal structure of Hsf putative domain 1 (PD1) is reported at 3.3 A resolution. The structure corrects the previous domain annotation by revealing the presence of an unexpected N-terminal TrpRing domain. PD1 represents the first Hsf domain to be solved, and thus paves the way for further research on the `hairpin-like' hypothesis.

The crystal structure of PD1, a Haemophilus surface fibril domain.,Wright J, Thomsen M, Kolodziejczyk R, Ridley J, Sinclair J, Carrington G, Singh B, Riesbeck K, Goldman A Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):101-108. doi:, 10.1107/S2053230X17001406. Epub 2017 Jan 31. PMID:28177321<ref>PMID:28177321</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lnl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Haemophilus influenzae]]
[[Category: Large Structures]]
[[Category: Goldman A]]
[[Category: Ridley J]]
[[Category: Thomsen M]]
[[Category: Wright J]]