|
|
| (9 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | {{Seed}} | |
| - | [[Image:1lv7.png|left|200px]] | |
| | | | |
| - | <!--
| + | ==Crystal Structure of the AAA domain of FtsH== |
| - | The line below this paragraph, containing "STRUCTURE_1lv7", creates the "Structure Box" on the page.
| + | <StructureSection load='1lv7' size='340' side='right'caption='[[1lv7]], [[Resolution|resolution]] 1.50Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1lv7]] is a 1 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=1LV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LV7 FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | -->
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | {{STRUCTURE_1lv7| PDB=1lv7 | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lv7 OCA], [https://pdbe.org/1lv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lv7 RCSB], [https://www.ebi.ac.uk/pdbsum/1lv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lv7 ProSAT]</span></td></tr> |
| - | | + | </table> |
| - | ===Crystal Structure of the AAA domain of FtsH===
| + | == 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> |
| - | | + | == Evolutionary Conservation == |
| - | <!-- | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_12176385}}, adds the Publication Abstract to the page
| + | Check<jmol> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 12176385 is the PubMed ID number.
| + | <jmolCheckbox> |
| - | -->
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lv/1lv7_consurf.spt"</scriptWhenChecked> |
| - | {{ABSTRACT_PUBMED_12176385}}
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==About this Structure== | + | </jmolCheckbox> |
| - | 1LV7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LV7 OCA].
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lv7 ConSurf]. |
| - | | + | <div style="clear:both"></div> |
| - | ==Reference== | + | == References == |
| - | The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution., Krzywda S, Brzozowski AM, Verma C, Karata K, Ogura T, Wilkinson AJ, Structure. 2002 Aug;10(8):1073-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12176385 12176385]
| + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Brzozowski, A M.]] | + | [[Category: Brzozowski AM]] |
| - | [[Category: Karata, K.]] | + | [[Category: Karata K]] |
| - | [[Category: Krzywda, S.]] | + | [[Category: Krzywda S]] |
| - | [[Category: Ogura, T.]] | + | [[Category: Ogura T]] |
| - | [[Category: Verma, C.]] | + | [[Category: Verma C]] |
| - | [[Category: Wilkinson, A J.]] | + | [[Category: Wilkinson AJ]] |
| - | [[Category: Alpha/beta domain]]
| + | |
| - | [[Category: Four helix bundle]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:24:07 2008''
| + | |
| Structural highlights
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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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:http://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:http://dx.doi.org/10.1128/JB.00871-08
|