2zpm: Difference between revisions
New page: '''Unreleased structure''' The entry 2zpm is ON HOLD Authors: Inaba, K. Description: Crystal structure analysis of PDZ domain B ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] o... |
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==Crystal structure analysis of PDZ domain B== | |||
<StructureSection load='2zpm' size='340' side='right'caption='[[2zpm]], [[Resolution|resolution]] 0.98Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2zpm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZPM FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=2zpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zpm OCA], [https://pdbe.org/2zpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zpm RCSB], [https://www.ebi.ac.uk/pdbsum/2zpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zpm 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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zp/2zpm_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2zpm ConSurf]. | |||
<div style="clear:both"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ecoli]] | |||
[[Category: Large Structures]] | |||
[[Category: Inaba, K]] | |||
[[Category: Suzuki, M]] | |||
[[Category: Hydrolase]] | |||
[[Category: Inner membrane]] | |||
[[Category: Membrane]] | |||
[[Category: Membrane protein]] | |||
[[Category: Metal-binding]] | |||
[[Category: Metalloprotease]] | |||
[[Category: Metalloproteinase]] | |||
[[Category: Pdz domain]] | |||
[[Category: Protease]] | |||
[[Category: Transmembrane]] | |||
[[Category: Zinc]] |
Latest revision as of 20:35, 15 December 2021
Crystal structure analysis of PDZ domain BCrystal structure analysis of PDZ domain B
Structural highlights
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] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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