7vhp: Difference between revisions

Latest revision as of 06:20, 19 June 2024

Structural insights into the membrane microdomain organization by SPFH family proteins

Structural highlights

7vhp is a 48 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.27Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FTSH_ECOLI Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, this probably requires ATP. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.^[1] ^[2] ^[3] ^[4] As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS).^[5] ^[6] ^[7] ^[8]

References

↑ Tomoyasu T, Gamer J, Bukau B, Kanemori M, Mori H, Rutman AJ, Oppenheim AB, Yura T, Yamanaka K, Niki H, et al.. Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. EMBO J. 1995 Jun 1;14(11):2551-60. PMID:7781608
↑ Kihara A, Akiyama Y, Ito K. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc Natl Acad Sci U S A. 1995 May 9;92(10):4532-6. PMID:7753838
↑ Ogura T, Inoue K, Tatsuta T, Suzaki T, Karata K, Young K, Su LH, Fierke CA, Jackman JE, Raetz CR, Coleman J, Tomoyasu T, Matsuzawa H. Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol Microbiol. 1999 Feb;31(3):833-44. PMID:10048027
↑ Katz C, Ron EZ. Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli. J Bacteriol. 2008 Nov;190(21):7117-22. doi: 10.1128/JB.00871-08. Epub 2008 Sep 5. PMID:18776015 doi:https://dx.doi.org/10.1128/JB.00871-08
↑ Tomoyasu T, Gamer J, Bukau B, Kanemori M, Mori H, Rutman AJ, Oppenheim AB, Yura T, Yamanaka K, Niki H, et al.. Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. EMBO J. 1995 Jun 1;14(11):2551-60. PMID:7781608
↑ Kihara A, Akiyama Y, Ito K. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc Natl Acad Sci U S A. 1995 May 9;92(10):4532-6. PMID:7753838
↑ Ogura T, Inoue K, Tatsuta T, Suzaki T, Karata K, Young K, Su LH, Fierke CA, Jackman JE, Raetz CR, Coleman J, Tomoyasu T, Matsuzawa H. Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol Microbiol. 1999 Feb;31(3):833-44. PMID:10048027
↑ Katz C, Ron EZ. Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli. J Bacteriol. 2008 Nov;190(21):7117-22. doi: 10.1128/JB.00871-08. Epub 2008 Sep 5. PMID:18776015 doi:https://dx.doi.org/10.1128/JB.00871-08

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Tomoyasu T, Gamer J, Bukau B, Kanemori M, Mori H, Rutman AJ, Oppenheim AB, Yura T, Yamanaka K, Niki H, et al.. Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. EMBO J. 1995 Jun 1;14(11):2551-60. PMID:7781608

[2] Kihara A, Akiyama Y, Ito K. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc Natl Acad Sci U S A. 1995 May 9;92(10):4532-6. PMID:7753838

[3] Ogura T, Inoue K, Tatsuta T, Suzaki T, Karata K, Young K, Su LH, Fierke CA, Jackman JE, Raetz CR, Coleman J, Tomoyasu T, Matsuzawa H. Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol Microbiol. 1999 Feb;31(3):833-44. PMID:10048027

[4] Katz C, Ron EZ. Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli. J Bacteriol. 2008 Nov;190(21):7117-22. doi: 10.1128/JB.00871-08. Epub 2008 Sep 5. PMID:18776015 doi:https://dx.doi.org/10.1128/JB.00871-08

[5] Tomoyasu T, Gamer J, Bukau B, Kanemori M, Mori H, Rutman AJ, Oppenheim AB, Yura T, Yamanaka K, Niki H, et al.. Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. EMBO J. 1995 Jun 1;14(11):2551-60. PMID:7781608

[6] Kihara A, Akiyama Y, Ito K. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc Natl Acad Sci U S A. 1995 May 9;92(10):4532-6. PMID:7753838

[7] Ogura T, Inoue K, Tatsuta T, Suzaki T, Karata K, Young K, Su LH, Fierke CA, Jackman JE, Raetz CR, Coleman J, Tomoyasu T, Matsuzawa H. Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol Microbiol. 1999 Feb;31(3):833-44. PMID:10048027

[8] Katz C, Ron EZ. Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli. J Bacteriol. 2008 Nov;190(21):7117-22. doi: 10.1128/JB.00871-08. Epub 2008 Sep 5. PMID:18776015 doi:https://dx.doi.org/10.1128/JB.00871-08

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-====
+==Structural insights into the membrane microdomain organization by SPFH family proteins==
-<StructureSection load='7vhp' size='340' side='right'caption='[[7vhp]]' scene=''>
+<StructureSection load='7vhp' size='340' side='right'caption='[[7vhp]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7vhp]] is a 48 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VHP 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=7vhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vhp OCA], [https://pdbe.org/7vhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vhp RCSB], [https://www.ebi.ac.uk/pdbsum/7vhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vhp ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.27&#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=7vhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vhp OCA], [https://pdbe.org/7vhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vhp RCSB], [https://www.ebi.ac.uk/pdbsum/7vhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vhp ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/FTSH_ECOLI FTSH_ECOLI] Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, this probably requires ATP. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.<ref>PMID:7781608</ref> <ref>PMID:7753838</ref> <ref>PMID:10048027</ref> <ref>PMID:18776015</ref>   As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS).<ref>PMID:7781608</ref> <ref>PMID:7753838</ref> <ref>PMID:10048027</ref> <ref>PMID:18776015</ref>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Z-disk]]
+[[Category: Gao N]]
+[[Category: Li NN]]
+[[Category: Luo DY]]
+[[Category: Ma CY]]
+[[Category: Wang CK]]
+[[Category: Yan L]]
+[[Category: Yang WX]]

7vhp: Difference between revisions

Latest revision as of 06:20, 19 June 2024

Structural insights into the membrane microdomain organization by SPFH family proteins

Structural highlights

Function

References

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