1pxv

From Proteopedia

(Difference between revisions)

Revision as of 08:34, 24 February 2018

The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease

Structural highlights

1pxv is a 4 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1nyc, 1cv8
Gene:	staphopain B ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885), staphostatin B ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SSPB_STAAU] Cysteine protease able to degrade elastin, fibrogen, fibronectin and kininogen. Exhibits a strong preference for substrates where arginine is preceded by a hydrophobic amino acid. Promotes detachment of primary human keratinocytes. Along with other extracellular proteases is involved in colonization and infection of human tissues (By similarity). [SSPC_STAA8] Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology.^[1] ^[2]

Publication Abstract from PubMed

Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Our recent crystal structure of staphostatin B has shown that this inhibitor forms a mixed, eight-stranded beta-barrel with statistically significant similarity to lipocalins, but not to cystatins. We now present the 1.8-A crystal structure of staphostatin B in complex with an inactive mutant of its target protease. The complex is held together through extensive interactions and buries a total surface area of 2300 A2. Unexpectedly for a cysteine protease inhibitor, staphostatin B binds to staphopain B in an almost substrate-like manner. The inhibitor polypeptide chain runs through the protease active site cleft in the forward direction, with residues IG-TS in P2 to P2' positions. Both in the free and complexed forms, the P1 glycine residue of the inhibitor is in a main chain conformation only accessible to glycines. Mutations in this residue lead to a loss of affinity of the inhibitor for protease and convert the inhibitor into a substrate.

The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease.,Filipek R, Rzychon M, Oleksy A, Gruca M, Dubin A, Potempa J, Bochtler M J Biol Chem. 2003 Oct 17;278(42):40959-66. Epub 2003 Jul 21. PMID:12874290^[3]

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

References

↑ Rzychon M, Sabat A, Kosowska K, Potempa J, Dubin A. Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases. Mol Microbiol. 2003 Aug;49(4):1051-66. PMID:12890028
↑ Shaw LN, Golonka E, Szmyd G, Foster SJ, Travis J, Potempa J. Cytoplasmic control of premature activation of a secreted protease zymogen: deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype. J Bacteriol. 2005 Mar;187(5):1751-62. PMID:15716447 doi:http://dx.doi.org/187/5/1751
↑ Filipek R, Rzychon M, Oleksy A, Gruca M, Dubin A, Potempa J, Bochtler M. The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease. J Biol Chem. 2003 Oct 17;278(42):40959-66. Epub 2003 Jul 21. PMID:12874290 doi:http://dx.doi.org/10.1074/jbc.M302926200

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/1pxv"

@@ Line 1: / Line 1: @@
 ==The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease==
 <StructureSection load='1pxv' size='340' side='right' caption='[[1pxv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nyc|1nyc]], [[1cv8|1cv8]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">staphopain B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885]), staphostatin B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=1pxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxv OCA], [http://pdbe.org/1pxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pxv RCSB], [http://www.ebi.ac.uk/pdbsum/1pxv PDBsum]</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=1pxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxv OCA], [http://pdbe.org/1pxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pxv RCSB], [http://www.ebi.ac.uk/pdbsum/1pxv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxv ProSAT]</span></td></tr>
 </table>
 == Function ==

1pxv

From Proteopedia

Revision as of 08:34, 24 February 2018

The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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