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| - | ==STRUCTURE OF E.COLI RHOMBOID PROTEASE GLPG ACTIVE SITE MUTANT, S201T IN TRIGONAL CRYSTAL FORM== | + | |
| - | <StructureSection load='2xtu' size='340' side='right' caption='[[2xtu]], [[Resolution|resolution]] 1.85Å' scene=''> | + | ==Structure of E.coli rhomboid protease GlpG active site mutant, S201T in trigonal crystal form== |
| | + | <StructureSection load='2xtu' size='340' side='right'caption='[[2xtu]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xtu]] 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=2XTU OCA]. <br> | + | <table><tr><td colspan='2'>[[2xtu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XTU FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene><br> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ic8|2ic8]], [[2xov|2xov]], [[2xow|2xow]], [[2irv|2irv]], [[2xtv|2xtv]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2xtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xtu OCA], [https://pdbe.org/2xtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xtu RCSB], [https://www.ebi.ac.uk/pdbsum/2xtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xtu ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xtu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xtu RCSB], [http://www.ebi.ac.uk/pdbsum/2xtu PDBsum]</span></td></tr> | + | </table> |
| - | <table> | + | == Function == |
| | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | Structure of rhomboid protease in a lipid environment.,Vinothkumar KR J Mol Biol. 2011 Mar 25;407(2):232-47. Epub 2011 Jan 19. PMID:21256137<ref>PMID:21256137</ref> | | Structure of rhomboid protease in a lipid environment.,Vinothkumar KR J Mol Biol. 2011 Mar 25;407(2):232-47. Epub 2011 Jan 19. PMID:21256137<ref>PMID:21256137</ref> |
| | | | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2xtu" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Rhomboid protease|Rhomboid protease]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli]] | + | [[Category: Large Structures]] |
| - | [[Category: Rhomboid protease]]
| + | [[Category: Vinothkumar KR]] |
| - | [[Category: Vinothkumar, K R.]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Membrane protein]]
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| Structural highlights
Function
GLPG_ECOLI Rhomboid-type serine protease that catalyzes intramembrane proteolysis.[1] [2]
Publication Abstract from PubMed
Structures of the prokaryotic homologue of rhomboid proteases reveal a core of six transmembrane helices, with the active-site residues residing in a hydrophilic cavity. The native environment of rhomboid protease is a lipid bilayer, yet all the structures determined thus far are in a nonnative detergent environment. There remains a possibility of structural artefacts arising from the use of detergents. In an attempt to address the effect of detergents on the structure of rhomboid protease, crystals of GlpG, an Escherichia coli rhomboid protease in a lipid environment, were obtained using two alternative approaches. The structure of GlpG refined to 1. 7-A resolution was obtained from crystals grown in the presence of lipid bicelles. This structure reveals well-ordered and partly ordered lipid molecules forming an annulus around the protein. Lipid molecules adapt to the surface features of protein and arrange such that they match the hydrophobic thickness of GlpG. Virtually identical two-dimensional crystals were also obtained after detergent removal by dialysis. A comparison of an equivalent structure determined in a completely delipidated detergent environment provides insights on how detergent substitutes for lipid. A detergent molecule is also observed close to the active site, helping to postulate a model for substrate binding and hydrolysis in rhomboids.
Structure of rhomboid protease in a lipid environment.,Vinothkumar KR J Mol Biol. 2011 Mar 25;407(2):232-47. Epub 2011 Jan 19. PMID:21256137[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wu Z, Yan N, Feng L, Oberstein A, Yan H, Baker RP, Gu L, Jeffrey PD, Urban S, Shi Y. Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry. Nat Struct Mol Biol. 2006 Dec;13(12):1084-91. Epub 2006 Nov 10. PMID:17099694 doi:10.1038/nsmb1179
- ↑ Maegawa S, Ito K, Akiyama Y. Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane. Biochemistry. 2005 Oct 18;44(41):13543-52. PMID:16216077 doi:10.1021/bi051363k
- ↑ Vinothkumar KR. Structure of rhomboid protease in a lipid environment. J Mol Biol. 2011 Mar 25;407(2):232-47. Epub 2011 Jan 19. PMID:21256137 doi:10.1016/j.jmb.2011.01.029
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