3id2: Difference between revisions

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<StructureSection load='3id2' size='340' side='right'caption='[[3id2]], [[Resolution|resolution]] 3.09&Aring;' scene=''>
<StructureSection load='3id2' size='340' side='right'caption='[[3id2]], [[Resolution|resolution]] 3.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3id2]] is a 2 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=3ID2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ID2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3id2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ID2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ID2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></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]] 3.089&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3id1|3id1]], [[3id3|3id3]], [[3id4|3id4]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rseP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3id2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3id2 OCA], [https://pdbe.org/3id2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3id2 RCSB], [https://www.ebi.ac.uk/pdbsum/3id2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3id2 ProSAT]</span></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=3id2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3id2 OCA], [https://pdbe.org/3id2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3id2 RCSB], [https://www.ebi.ac.uk/pdbsum/3id2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3id2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Feng, L]]
[[Category: Feng L]]
[[Category: Li, X]]
[[Category: Li X]]
[[Category: Shi, Y]]
[[Category: Shi Y]]
[[Category: Wang, B]]
[[Category: Wang B]]
[[Category: Wang, J]]
[[Category: Wang J]]
[[Category: Cell inner membrane]]
[[Category: Cell membrane]]
[[Category: Hydrolase]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Metalloprotease]]
[[Category: Protease]]
[[Category: Transmembrane]]
[[Category: Zinc]]
Retrieved from "https://proteopedia.org/3id2"