3wqb

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of aeromonas sobria serine protease (ASP) and the chaperone (ORF2) complex

Structural highlights

3wqb is a 2 chain structure with sequence from Aeromonas sobria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.41Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Publication Abstract from PubMed

Subtilisin-like proteases are broadly expressed in organisms ranging from bacteria to mammals. During maturation of these enzymes, N-terminal propeptides function as intramolecular chaperones, assisting the folding of their catalytic domains. However, we have identified an exceptional case, the serine protease from Aeromonas sobria (ASP), that lacks a propeptide. Instead, ORF2, a protein encoded just downstream of asp, appears essential for proper ASP folding. The mechanism by which ORF2 functions remains an open question, because it shares no sequence homology with any known intramolecular propeptide or other protein. Here we report the crystal structure of the ORF2-ASP complex and the solution structure of free ORF2. ORF2 consists of three regions: an N-terminal extension, a central body, and a C-terminal tail. Together, the structure of the central body and the C-terminal tail is similar to that of the intramolecular propeptide. The N-terminal extension, which is not seen in other subtilisin-like enzymes, is intrinsically disordered but forms some degree of secondary structure upon binding ASP. We also show that C-terminal (DeltaC1 and DeltaC5) or N-terminal (DeltaN43 and DeltaN64) deletion eliminates the ability of ORF2 to function as a chaperone. Characterization of the maturation of ASP with ORF2 showed that folding occurs in the periplasmic space and is followed by translocation into extracellular space and dissociation from ORF2, generating active ASP. Finally, a PSI-BLAST search revealed that operons encoding subtilases and their external chaperones are widely distributed among Gram-negative bacteria, suggesting that ASP and its homologs form a novel family of subtilases having an external chaperone.

Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria.,Kobayashi H, Yoshida T, Miyakawa T, Tashiro M, Okamoto K, Yamanaka H, Tanokura M, Tsuge H J Biol Chem. 2015 Apr 24;290(17):11130-43. doi: 10.1074/jbc.M114.622852. Epub, 2015 Mar 16. PMID:25784551^[10]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Okamoto K, Nomura T, Hamada M, Fukuda T, Noguchi Y, Fujii Y. Production of serine protease of Aeromonas sobria is controlled by the protein encoded by the gene lying adjacent to the 3' end of the protease gene. Microbiol Immunol. 2000;44(9):787-98. PMID:11092244 doi:10.1111/j.1348-0421.2000.tb02565.x
↑ Yokoyama R, Fujii Y, Noguchi Y, Nomura T, Akita M, Setsu K, Yamamoto S, Okamoto K. Physicochemical and biological properties of an extracellular serine protease of Aeromonas sobria. Microbiol Immunol. 2002;46(6):383-90. PMID:12153115 doi:10.1111/j.1348-0421.2002.tb02710.x
↑ Kobayashi H, Takahashi E, Oguma K, Fujii Y, Yamanaka H, Negishi T, Arimoto-Kobayashi S, Tsuji T, Okamoto K. Cleavage specificity of the serine protease of Aeromonas sobria, a member of the kexin family of subtilases. FEMS Microbiol Lett. 2006 Mar;256(1):165-70. PMID:16487335 doi:10.1111/j.1574-6968.2006.00134.x
↑ Imamura T, Kobayashi H, Khan R, Nitta H, Okamoto K. Induction of vascular leakage and blood pressure lowering through kinin release by a serine proteinase from Aeromonas sobria. J Immunol. 2006 Dec 15;177(12):8723-9. PMID:17142774 doi:10.4049/jimmunol.177.12.8723
↑ Nitta H, Kobayashi H, Irie A, Baba H, Okamoto K, Imamura T. Activation of prothrombin by ASP, a serine protease released from Aeromonas sobria. FEBS Lett. 2007 Dec 22;581(30):5935-9. PMID:18067862 doi:10.1016/j.febslet.2007.11.076
↑ Imamura T, Nitta H, Wada Y, Kobayashi H, Okamoto K. Impaired plasma clottability induction through fibrinogen degradation by ASP, a serine protease released from Aeromonas sobria. FEMS Microbiol Lett. 2008 Jul;284(1):35-42. PMID:18462393 doi:10.1111/j.1574-6968.2008.01184.x
↑ Nitta H, Imamura T, Wada Y, Irie A, Kobayashi H, Okamoto K, Baba H. Production of C5a by ASP, a serine protease released from Aeromonas sobria. J Immunol. 2008 Sep 1;181(5):3602-8. PMID:18714034 doi:10.4049/jimmunol.181.5.3602
↑ Kobayashi H, Utsunomiya H, Yamanaka H, Sei Y, Katunuma N, Okamoto K, Tsuge H. Structural basis for the kexin-like serine protease from Aeromonas sobria as sepsis-causing factor. J Biol Chem. 2009 Oct 2;284(40):27655-63. Epub 2009 Aug 4. PMID:19654332 doi:10.1074/jbc.M109.006114
↑ Kobayashi H, Yoshida T, Miyakawa T, Tashiro M, Okamoto K, Yamanaka H, Tanokura M, Tsuge H. Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. J Biol Chem. 2015 Apr 24;290(17):11130-43. doi: 10.1074/jbc.M114.622852. Epub, 2015 Mar 16. PMID:25784551 doi:http://dx.doi.org/10.1074/jbc.M114.622852
↑ Kobayashi H, Yoshida T, Miyakawa T, Tashiro M, Okamoto K, Yamanaka H, Tanokura M, Tsuge H. Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. J Biol Chem. 2015 Apr 24;290(17):11130-43. doi: 10.1074/jbc.M114.622852. Epub, 2015 Mar 16. PMID:25784551 doi:http://dx.doi.org/10.1074/jbc.M114.622852

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3wqb"

@@ Line 3: / Line 3: @@
 <StructureSection load='3wqb' size='340' side='right'caption='[[3wqb]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
 == 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>
 </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;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Aerso]]
+[[Category: Aeromonas sobria]]
 [[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]]

3wqb

From Proteopedia

Current revision

Crystal structure of aeromonas sobria serine protease (ASP) and the chaperone (ORF2) complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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