Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Structure of the secretion domain of HxuA from Haemophilus influenzae

Structure of the secretion domain of HxuA from Haemophilus influenzae 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 Å resolution structure of the secretion domain of HxuA, HxuA301, is reported. The structure reveals that HxuA301 folds into a β‐helix domain with two extra‐helical motifs, a four‐stranded β‐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 β‐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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Structure of the secretion domain of HxuA from Haemophilus influenzae

Loading next page...
 
/lp/wiley/structure-of-the-secretion-domain-of-hxua-from-haemophilus-influenzae-xklU03KEd5

References (36)

Publisher
Wiley
Copyright
International Union of Crystallography, 2013
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S174430911302962X
pmid
24316822
Publisher site
See Article on Publisher Site

Abstract

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 Å resolution structure of the secretion domain of HxuA, HxuA301, is reported. The structure reveals that HxuA301 folds into a β‐helix domain with two extra‐helical motifs, a four‐stranded β‐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 β‐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.

Journal

Acta Crystallographica Section FWiley

Published: Dec 1, 2013

There are no references for this article.