3wqb: Difference between revisions

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<StructureSection load='3wqb' size='340' side='right'caption='[[3wqb]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
<StructureSection load='3wqb' size='340' side='right'caption='[[3wqb]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3wqb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aerso Aerso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WQB FirstGlance]. <br>
<table><tr><td colspan='2'>[[3wqb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_sobria Aeromonas sobria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WQB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.41&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2oxa|2oxa]], [[2mk4|2mk4]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3wqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wqb OCA], [https://pdbe.org/3wqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wqb RCSB], [https://www.ebi.ac.uk/pdbsum/3wqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wqb ProSAT]</span></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=3wqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wqb OCA], [https://pdbe.org/3wqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wqb RCSB], [https://www.ebi.ac.uk/pdbsum/3wqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wqb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ASP_AERSO ASP_AERSO] Exhibits serine protease activity (PubMed:11092244, PubMed:12153115, PubMed:16487335, PubMed:18067862, PubMed:18462393, PubMed:19654332). Preferentially cleaves the peptide bond following two basic residues, one of which is Lys, but does not recognize the bond following a single basic residue (PubMed:16487335). Probable potent virulence factor that cleaves various host plasma proteins, including prekallikrein, prothrombin and fibrinogen (PubMed:16487335, PubMed:17142774, PubMed:18067862, PubMed:18462393, PubMed:19654332). ASP induces vascular leakage and reduction in blood pressure by activating the host plasma kallikrein/kinin system (PubMed:12153115, PubMed:16487335, PubMed:17142774). It affects the host coagulation system during infection through activation of prothrombin to alpha-thrombin and degradation of fibrinogen, which impairs plasma clottability (PubMed:18067862, PubMed:18462393). It also hydrolyzes the complement component C5, releasing the C5a anaphylatoxin, which causes the formation of pus and edema (PubMed:18714034). In addition, degrades its external chaperone ORF2 after the secretion of the ASP-ORF2 complex (PubMed:25784551).<ref>PMID:11092244</ref> <ref>PMID:12153115</ref> <ref>PMID:16487335</ref> <ref>PMID:17142774</ref> <ref>PMID:18067862</ref> <ref>PMID:18462393</ref> <ref>PMID:18714034</ref> <ref>PMID:19654332</ref> <ref>PMID:25784551</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aerso]]
[[Category: Aeromonas sobria]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kato, R]]
[[Category: Kato R]]
[[Category: Kobayashi, H]]
[[Category: Kobayashi H]]
[[Category: Miyakawa, T]]
[[Category: Miyakawa T]]
[[Category: Tanokura, M]]
[[Category: Tanokura M]]
[[Category: Tashiro, M]]
[[Category: Tashiro M]]
[[Category: Tsuge, H]]
[[Category: Tsuge H]]
[[Category: Yamanaka, H]]
[[Category: Yamanaka H]]
[[Category: Yoshida, T]]
[[Category: Yoshida T]]
[[Category: Asp]]
[[Category: Calcium binding]]
[[Category: Chaperone]]
[[Category: Extracellular space]]
[[Category: Hydrolase-chaperone complex]]
[[Category: Orf2]]
[[Category: Serine protease]]