1rwr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1rwr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rwr, resolution 1.72&Aring;" /> '''Crystal structure of...)
Current revision (13:29, 13 March 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1rwr.gif|left|200px]]<br /><applet load="1rwr" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1rwr, resolution 1.72&Aring;" />
 
-
'''Crystal structure of filamentous hemagglutinin secretion domain'''<br />
 
-
==Overview==
+
==Crystal structure of filamentous hemagglutinin secretion domain==
-
Filamentous hemagglutinin (FHA), the major 230-kDa adhesin of the whooping, cough agent Bordetella pertussis, is one of the most efficiently secreted, proteins in Gram-negative bacteria. FHA is secreted by means of the, two-partner secretion (TPS) pathway. Several important human, animal, and, plant pathogens also secrete adhesins and other virulence factors by using, this mode of secretion. A TPS system is composed of two separate proteins, with TpsA the secreted protein and TpsB its associated specific, outermembrane transporter. All TPS-secreted proteins contain a distinctive, N-proximal module essential for secretion, the TPS domain. We report here, the 1.7- A structure of a functionally secreted 30-kDa N-terminal fragment, of FHA. It reveals that the TPS domain folds into a beta-helix, with three, extrahelical motifs, a beta-hairpin, a four-stranded beta-sheet, and an, N-terminal capping, mostly formed by the nonconserved regions of the TPS, domain. The structure thus explains why the TPS domain is able to initiate, folding of the beta-helical motifs that form the central domain of the, adhesin, because it is itself a beta-helical scaffold. It also contains, less conserved extrahelical regions most likely involved in specific, properties, such as the recognition of the outer-membrane transporter., This structure is representative of the TPS domains found so far in &gt;100, secreted proteins from pathogenic bacteria. It also provides a mechanistic, insight into how protein folding may be linked to secretion in the TPS, pathway.
+
<StructureSection load='1rwr' size='340' side='right'caption='[[1rwr]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1rwr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RWR 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]] 1.72&#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=1rwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rwr OCA], [https://pdbe.org/1rwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rwr RCSB], [https://www.ebi.ac.uk/pdbsum/1rwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rwr ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FHAB_BORPE FHAB_BORPE] Evidence for a role in host-cell binding and infection.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rw/1rwr_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rwr ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1RWR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RWR OCA].
+
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway., Clantin B, Hodak H, Willery E, Locht C, Jacob-Dubuisson F, Villeret V, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6194-9. Epub 2004 Apr 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15079085 15079085]
+
[[Category: Bordetella pertussis]]
[[Category: Bordetella pertussis]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Clantin, B.]]
+
[[Category: Clantin B]]
-
[[Category: Villeret, V.]]
+
[[Category: Villeret V]]
-
[[Category: adhesins]]
+
-
[[Category: beta-helix]]
+
-
[[Category: filamentous hemagglutinin]]
+
-
[[Category: tps domain]]
+
-
[[Category: type v secretion]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:54:36 2007''
+

Current revision

Crystal structure of filamentous hemagglutinin secretion domain

PDB ID 1rwr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rwr"
Personal tools