4i84
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==The crystal structure of the Haemophilus influenzae HxuA secretion domain involved in the two-partner secretion pathway== | |
| - | + | <StructureSection load='4i84' size='340' side='right' caption='[[4i84]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4i84]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Haein Haein]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I84 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I84 FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HI_0264, hxuA, KW20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 HAEIN])</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=4i84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i84 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i84 RCSB], [http://www.ebi.ac.uk/pdbsum/4i84 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/HXUA1_HAEIN HXUA1_HAEIN]] Binds heme/hemopexin complexes. | [[http://www.uniprot.org/uniprot/HXUA1_HAEIN HXUA1_HAEIN]] Binds heme/hemopexin complexes. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Haemophilus influenzae HxuA is a cell-surface protein with haem-haemopexin binding activity which is key to haem acquisition from haemopexin and thus is one of the potential sources of haem for this microorganism. HxuA is secreted by its specific transporter HxuB. HxuA/HxuB belongs to the so-called two-partner secretion systems (TPSs) that are characterized by a conserved N-terminal domain in the secreted protein which is essential for secretion. Here, the 1.5 A resolution structure of the secretion domain of HxuA, HxuA301, is reported. The structure reveals that HxuA301 folds into a beta-helix domain with two extra-helical motifs, a four-stranded beta-sheet and an N-terminal cap. Comparisons with other structures of TpsA secretion domains are reported. They reveal that despite limited sequence identity, strong structural similarities are found between the beta-helix motifs, consistent with the idea that the TPS domain plays a role not only in the interaction with the specific TpsB partners but also as the scaffold initiating progressive folding of the TpsA proteins at the bacterial surface. | ||
| - | + | Structure of the secretion domain of HxuA from Haemophilus influenzae.,Baelen S, Dewitte F, Clantin B, Villeret V Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1322-7. doi:, 10.1107/S174430911302962X. Epub 2013 Nov 28. PMID:24316822<ref>PMID:24316822</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Haein]] | [[Category: Haein]] | ||
| - | [[Category: Baelen, S | + | [[Category: Baelen, S]] |
| - | [[Category: Clantin, B | + | [[Category: Clantin, B]] |
| - | [[Category: Dewitte, F | + | [[Category: Dewitte, F]] |
| - | [[Category: Villeret, V | + | [[Category: Villeret, V]] |
[[Category: Beta-helix]] | [[Category: Beta-helix]] | ||
[[Category: Hxub]] | [[Category: Hxub]] | ||
[[Category: Protein transport]] | [[Category: Protein transport]] | ||
[[Category: Two-partner secretion pathway]] | [[Category: Two-partner secretion pathway]] | ||
Revision as of 12:53, 25 December 2014
The crystal structure of the Haemophilus influenzae HxuA secretion domain involved in the two-partner secretion pathway
| |||||||||||
