7w71

From Proteopedia

(Difference between revisions)

Revision as of 17:37, 29 November 2023

Crystal structure of the PDZ-C domain of E. coli RseP in complex with 12C7 Fab

Structural highlights

7w71 is a 6 chain structure with sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RSEP_ECOLI A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue "Val-148" of RseA may be required for this. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. Can also cleave sequences in transmembrane regions of other proteins (such as LacY) as well as liberated signal peptides of beta-lactamase, OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lpp and TorA, probably within the membrane.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

Site-2 proteases are a conserved family of intramembrane proteases that cleave transmembrane substrates to regulate signal transduction and maintain proteostasis. Here, we elucidated crystal structures of inhibitor-bound forms of bacterial site-2 proteases including Escherichia coli RseP. Structure-based chemical modification and cross-linking experiments indicated that the RseP domains surrounding the active center undergo conformational changes to expose the substrate-binding site, suggesting that RseP has a gating mechanism to regulate substrate entry. Furthermore, mutational analysis suggests that a conserved electrostatic linkage between the transmembrane and peripheral membrane-associated domains mediates the conformational changes. In vivo cleavage assays also support that the substrate transmembrane helix is unwound by strand addition to the intramembrane beta sheet of RseP and is clamped by a conserved asparagine residue at the active center for efficient cleavage. This mechanism underlying the substrate binding, i.e., unwinding and clamping, appears common across distinct families of intramembrane proteases that cleave transmembrane segments.

Mechanistic insights into intramembrane proteolysis by E. coli site-2 protease homolog RseP.,Imaizumi Y, Takanuki K, Miyake T, Takemoto M, Hirata K, Hirose M, Oi R, Kobayashi T, Miyoshi K, Aruga R, Yokoyama T, Katagiri S, Matsuura H, Iwasaki K, Kato T, Kaneko MK, Kato Y, Tajiri M, Akashi S, Nureki O, Hizukuri Y, Akiyama Y, Nogi T Sci Adv. 2022 Aug 26;8(34):eabp9011. doi: 10.1126/sciadv.abp9011. Epub 2022 Aug, 24. PMID:36001659^[8]

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

References

↑ Kanehara K, Akiyama Y, Ito K. Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli. Gene. 2001 Dec 27;281(1-2):71-9. PMID:11750129
↑ Kanehara K, Ito K, Akiyama Y. YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA. Genes Dev. 2002 Aug 15;16(16):2147-55. PMID:12183368 doi:http://dx.doi.org/10.1101/gad.1002302
↑ Alba BM, Leeds JA, Onufryk C, Lu CZ, Gross CA. DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma(E)-dependent extracytoplasmic stress response. Genes Dev. 2002 Aug 15;16(16):2156-68. PMID:12183369 doi:10.1101/gad.1008902
↑ Akiyama Y, Kanehara K, Ito K. RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences. EMBO J. 2004 Nov 10;23(22):4434-42. Epub 2004 Oct 21. PMID:15496982 doi:http://dx.doi.org/7600449
↑ Koide K, Ito K, Akiyama Y. Substrate recognition and binding by RseP, an Escherichia coli intramembrane protease. J Biol Chem. 2008 Apr 11;283(15):9562-70. doi: 10.1074/jbc.M709984200. Epub 2008 , Feb 11. PMID:18268014 doi:http://dx.doi.org/10.1074/jbc.M709984200
↑ Saito A, Hizukuri Y, Matsuo E, Chiba S, Mori H, Nishimura O, Ito K, Akiyama Y. Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria. Proc Natl Acad Sci U S A. 2011 Aug 16;108(33):13740-5. doi:, 10.1073/pnas.1108376108. Epub 2011 Aug 2. PMID:21810987 doi:http://dx.doi.org/10.1073/pnas.1108376108
↑ Inaba K, Suzuki M, Maegawa K, Akiyama S, Ito K, Akiyama Y. A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli. J Biol Chem. 2008 Dec 12;283(50):35042-52. doi: 10.1074/jbc.M806603200. Epub 2008, Oct 22. PMID:18945679 doi:http://dx.doi.org/10.1074/jbc.M806603200
↑ Imaizumi Y, Takanuki K, Miyake T, Takemoto M, Hirata K, Hirose M, Oi R, Kobayashi T, Miyoshi K, Aruga R, Yokoyama T, Katagiri S, Matsuura H, Iwasaki K, Kato T, Kaneko MK, Kato Y, Tajiri M, Akashi S, Nureki O, Hizukuri Y, Akiyama Y, Nogi T. Mechanistic insights into intramembrane proteolysis by E. coli site-2 protease homolog RseP. Sci Adv. 2022 Aug 26;8(34):eabp9011. doi: 10.1126/sciadv.abp9011. Epub 2022 Aug, 24. PMID:36001659 doi:http://dx.doi.org/10.1126/sciadv.abp9011

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/7w71"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[7w71]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W71 FirstGlance]. <br>
-</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=7w71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w71 OCA], [https://pdbe.org/7w71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w71 RCSB], [https://www.ebi.ac.uk/pdbsum/7w71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w71 ProSAT]</span></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]] 3.2&#8491;</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=7w71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w71 OCA], [https://pdbe.org/7w71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w71 RCSB], [https://www.ebi.ac.uk/pdbsum/7w71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w71 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RSEP_ECOLI RSEP_ECOLI]] A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue "Val-148" of RseA may be required for this. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. Can also cleave sequences in transmembrane regions of other proteins (such as LacY) as well as liberated signal peptides of beta-lactamase, OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lpp and TorA, probably within the membrane.<ref>PMID:11750129</ref> <ref>PMID:12183368</ref> <ref>PMID:12183369</ref> <ref>PMID:15496982</ref> <ref>PMID:18268014</ref> <ref>PMID:21810987</ref> <ref>PMID:18945679</ref>
+[https://www.uniprot.org/uniprot/RSEP_ECOLI RSEP_ECOLI] A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue "Val-148" of RseA may be required for this. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. Can also cleave sequences in transmembrane regions of other proteins (such as LacY) as well as liberated signal peptides of beta-lactamase, OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lpp and TorA, probably within the membrane.<ref>PMID:11750129</ref> <ref>PMID:12183368</ref> <ref>PMID:12183369</ref> <ref>PMID:15496982</ref> <ref>PMID:18268014</ref> <ref>PMID:21810987</ref> <ref>PMID:18945679</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

7w71

From Proteopedia

Revision as of 17:37, 29 November 2023

Crystal structure of the PDZ-C domain of E. coli RseP in complex with 12C7 Fab

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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