4hdd
From Proteopedia
(Difference between revisions)
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- | + | ==Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease== | |
- | + | <StructureSection load='4hdd' size='340' side='right' caption='[[4hdd]], [[Resolution|resolution]] 1.35Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[4hdd]] is a 1 chain structure with 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=4HDD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HDD FirstGlance]. <br> | |
- | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> |
+ | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lep|2lep]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b3424, glpG, JW5687 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Rhomboid_protease Rhomboid protease], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hdd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hdd RCSB], [http://www.ebi.ac.uk/pdbsum/4hdd PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
[[http://www.uniprot.org/uniprot/GLPG_ECOLI GLPG_ECOLI]] Rhomboid-type serine protease that catalyzes intramembrane proteolysis.<ref>PMID:17099694</ref> <ref>PMID:16216077</ref> | [[http://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 == | ||
+ | Rhomboids are membrane-embedded serine proteases that cleave membrane protein substrates. Escherichia coli rhomboid GlpG (ecGlpG) consists of an N-terminal cytoplasmic domain and a membrane domain containing the active site. We determined the crystal structure of the soluble cytoplasmic domain of ecGlpG at 1.35A resolution and examined whether this domain affected the catalytic activity of the enzyme. The structure revealed that the ecGlpG cytoplasmic domain exists as a dimer with extensive domain swapping between the two monomers. Domain-swapped dimers can be isolated from the full-length protein, suggesting that this is a physiologically relevant structure. An extensive steady-state kinetic analysis of the full-length ecGlpG and its membrane domain using soluble and transmembrane model protein substrates resulted in an unexpected conclusion: removal of the cytoplasmic domain does not alter the catalytic parameters for detergent-solubilized rhomboid for both substrates. | ||
- | + | Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease.,Lazareno-Saez C, Arutyunova E, Coquelle N, Lemieux MJ J Mol Biol. 2013 Apr 12;425(7):1127-42. doi: 10.1016/j.jmb.2013.01.019. Epub 2013, Jan 23. PMID:23353827<ref>PMID:23353827</ref> | |
- | + | ||
- | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | + | </div> | |
+ | |||
+ | ==See Also== | ||
+ | *[[Rhomboid protease|Rhomboid protease]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Rhomboid protease]] | [[Category: Rhomboid protease]] | ||
- | [[Category: Arutyunova, E | + | [[Category: Arutyunova, E]] |
- | [[Category: Coquelle, N | + | [[Category: Coquelle, N]] |
- | [[Category: Lazareno-Saez, C | + | [[Category: Lazareno-Saez, C]] |
- | [[Category: Lemieux, M J | + | [[Category: Lemieux, M J]] |
[[Category: Domain swapping]] | [[Category: Domain swapping]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
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[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Peptidase]] | [[Category: Peptidase]] | ||
- | [[Category: Rhomboid protease]] |
Revision as of 22:06, 24 December 2014
Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease
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