1qy6

From Proteopedia

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Revision as of 10:06, 15 September 2021

Structue of V8 Protease from Staphylococcus aureus

Structural highlights

1qy6 is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus mu50. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Glutamyl endopeptidase, with EC number 3.4.21.19
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SSPA_STAAM] Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

V8 protease, an extracellular protease of Staphylococcus aureus, is related to the pancreatic serine proteases. The enzyme cleaves peptide bonds exclusively on the carbonyl side of aspartate and glutamate residues. Unlike the pancreatic serine proteases, V8 protease possesses no disulfide bridges. This is a major evolutionary difference, as all pancreatic proteases have at least two disulfide bridges. The structure of V8 protease shows structural similarity with several other serine proteases, specifically the epidermolytic toxins A and B from S. aureus and trypsin, in which the conformation of the active site is almost identical. V8 protease is also unique in that the positively charged N-terminus is involved in determining the substrate-specificity of the enzyme.

The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus.,Prasad L, Leduc Y, Hayakawa K, Delbaere LT Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):256-9. Epub 2004, Jan 23. PMID:14747701^[1]

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

References

↑ Prasad L, Leduc Y, Hayakawa K, Delbaere LT. The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus. Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):256-9. Epub 2004, Jan 23. PMID:14747701 doi:http://dx.doi.org/10.1107/S090744490302599X

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qy6"

@@ Line 3: / Line 3: @@
 <StructureSection load='1qy6' size='340' side='right'caption='[[1qy6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qy6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_mu50 Staphylococcus aureus subsp. aureus mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QY6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qy6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_mu50 Staphylococcus aureus subsp. aureus mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QY6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamyl_endopeptidase Glutamyl endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.19 3.4.21.19] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamyl_endopeptidase Glutamyl endopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.19 3.4.21.19] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qy6 OCA], [http://pdbe.org/1qy6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qy6 RCSB], [http://www.ebi.ac.uk/pdbsum/1qy6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qy6 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=1qy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qy6 OCA], [https://pdbe.org/1qy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qy6 RCSB], [https://www.ebi.ac.uk/pdbsum/1qy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qy6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SSPA_STAAM SSPA_STAAM]] Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).
+[[https://www.uniprot.org/uniprot/SSPA_STAAM SSPA_STAAM]] Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1qy6

From Proteopedia

Revision as of 10:06, 15 September 2021

Structue of V8 Protease from Staphylococcus aureus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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