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2lep

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Solution Structure of N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Escherichia Coli

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Categories: Escherichia coli | Large Structures | Ghasriani H | Goto NK | Sherratt AR

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 ==Solution Structure of N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Escherichia Coli==
-<StructureSection load='2lep' size='340' side='right'caption='[[2lep]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2lep' size='340' side='right'caption='[[2lep]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2lep]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LEP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2lep]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LEP FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glpG1, ECs4267 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Rhomboid_protease Rhomboid protease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.105 3.4.21.105] </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=2lep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lep OCA], [https://pdbe.org/2lep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lep RCSB], [https://www.ebi.ac.uk/pdbsum/2lep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lep ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/C3SPT7_ECOLX C3SPT7_ECOLX]] Rhomboid-type serine protease that catalyzes intramembrane proteolysis (By similarity).[HAMAP-Rule:MF_01594]
+[https://www.uniprot.org/uniprot/GLPG_ECOLI GLPG_ECOLI] Rhomboid-type serine protease that catalyzes intramembrane proteolysis.<ref>PMID:17099694</ref> <ref>PMID:16216077</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Rhomboid proteins comprise the largest class of intramembrane protease known, being conserved from bacteria to humans. The functional status of these proteases is typically assessed through direct or indirect detection of peptide cleavage products. Although these assays can report on the ability of a rhomboid to catalyze peptide bond cleavage, differences in measured hydrolysis rates can reflect changes in the structure and activity of catalytic residues, as well as the ability of the substrate to access the active site. Here we show that a highly reactive and sterically unencumbered fluorophosphonate activity-based protein profiling probe can be used to report on the catalytic integrity of active site residues in the Escherichia coli GlpG protein. We used results obtained with this probe on GlpG in proteomic samples, in combination with a conventional assay of proteolytic function on purified samples, to identify residues that are located on the cytoplasmic side of the lipid bilayer that are required for maximal proteolytic activity. Regions tested include the 90-residue aqueous-exposed N-terminus that encompasses a globular structure that we have determined by solution nuclear magnetic resonance, along with residues on the cytoplasmic side of the transmembrane domain core. While in most cases mutation or elimination of these residues did not significantly alter the catalytic status of the GlpG active site, the lipid-facing residue Arg227 was found to be important for maintaining a catalytically competent active site. In addition, we found a functionally critical region outside the transmembrane domain (TMD) core that is required for maximal protease activity. This region encompasses an additional 8-10 residues on the N-terminal side of the TMD core that precedes the first transmembrane segment and was not previously known to play a role in rhomboid function. These findings highlight the utility of the activity-based protein profiling approach for the characterization of rhomboid function.
-Activity-Based Protein Profiling of the Escherichia coli GlpG Rhomboid Protein Delineates the Catalytic Core.,Sherratt AR, Blais DR, Ghasriani H, Pezacki JP, Goto NK Biochemistry. 2012 Sep 21. PMID:22963263<ref>PMID:22963263</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2lep" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 16: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Rhomboid protease]]
+[[Category: Ghasriani H]]
-[[Category: Ghasriani, H]]
+[[Category: Goto NK]]
-[[Category: Goto, N K]]
+[[Category: Sherratt AR]]
-[[Category: Sherratt, A R]]
-[[Category: Cell membrane]]
-[[Category: Cytosol]]
-[[Category: Domain swapping]]
-[[Category: Hydrolase]]
-[[Category: Membrane protein]]
-[[Category: Micelle]]
-[[Category: Serine protease]]

2lep

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Solution Structure of N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Escherichia Coli

Structural highlights

Function

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References

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