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==CRYSTAL STRUCTURE OF TIP-ALPHA N34 (HP0596) FROM HELICOBACTER PYLORI AT PH4== | |||
[[ | <StructureSection load='2wcq' size='340' side='right' caption='[[2wcq]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2wcq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WCQ OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wcr|2wcr]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wcq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wcq RCSB], [http://www.ebi.ac.uk/pdbsum/2wcq PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Helicobacter pylori secretes a unique virulence factor, Tipalpha, that enters gastric cells and both stimulates the production of the TNF-alpha and activates the NF-kappaB pathway. The structures of a truncated version of Tipalpha (TipalphaN34) in two crystal forms are presented here. Tipalpha adopts a novel beta(1)alpha(1)alpha(2)beta(2)beta(3)alpha(3)alpha(4) topology that can be described as a combination of three domains. A first region consists in a short flexible extension, a second displays a dodecin-like fold and a third is a helical bundle domain similar to the sterile alpha motif (SAM). Analysis of the oligomerisation states of TipalphaN34 in the crystals and in solution suggests that the disulfide bridges could hold together Tipalpha monomers during their secretion in the gastric environment. | |||
Structures of the tumor necrosis factor alpha inducing protein Tipalpha: a novel virulence factor from Helicobacter pylori.,Tosi T, Cioci G, Jouravleva K, Dian C, Terradot L FEBS Lett. 2009 May 19;583(10):1581-5. Epub 2009 May 4. PMID:19401200<ref>PMID:19401200</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Cioci, G.]] | [[Category: Cioci, G.]] | ||
| Line 34: | Line 30: | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Tip-alpha]] | [[Category: Tip-alpha]] | ||
Revision as of 11:36, 7 May 2014
CRYSTAL STRUCTURE OF TIP-ALPHA N34 (HP0596) FROM HELICOBACTER PYLORI AT PH4CRYSTAL STRUCTURE OF TIP-ALPHA N34 (HP0596) FROM HELICOBACTER PYLORI AT PH4
Structural highlights
Publication Abstract from PubMedHelicobacter pylori secretes a unique virulence factor, Tipalpha, that enters gastric cells and both stimulates the production of the TNF-alpha and activates the NF-kappaB pathway. The structures of a truncated version of Tipalpha (TipalphaN34) in two crystal forms are presented here. Tipalpha adopts a novel beta(1)alpha(1)alpha(2)beta(2)beta(3)alpha(3)alpha(4) topology that can be described as a combination of three domains. A first region consists in a short flexible extension, a second displays a dodecin-like fold and a third is a helical bundle domain similar to the sterile alpha motif (SAM). Analysis of the oligomerisation states of TipalphaN34 in the crystals and in solution suggests that the disulfide bridges could hold together Tipalpha monomers during their secretion in the gastric environment. Structures of the tumor necrosis factor alpha inducing protein Tipalpha: a novel virulence factor from Helicobacter pylori.,Tosi T, Cioci G, Jouravleva K, Dian C, Terradot L FEBS Lett. 2009 May 19;583(10):1581-5. Epub 2009 May 4. PMID:19401200[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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