3ubb: Difference between revisions
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<StructureSection load='3ubb' size='340' side='right'caption='[[3ubb]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='3ubb' size='340' side='right'caption='[[3ubb]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ubb]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ubb]] is a 1 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=3UBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UBB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.601Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3UB:PROPAN-2-YL+HYDROGEN+(S)-[(1R)-1-{[(BENZYLOXY)CARBONYL]AMINO}ETHYL]PHOSPHONATE'>3UB</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=3ubb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ubb OCA], [https://pdbe.org/3ubb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ubb RCSB], [https://www.ebi.ac.uk/pdbsum/3ubb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ubb ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ha Y]] | |||
[[Category: Ha | [[Category: Xue Y]] | ||
[[Category: Xue | |||
Latest revision as of 12:45, 30 October 2024
The crystal structure of GlpG in complex with a phosphonofluoridate inhibitorThe crystal structure of GlpG in complex with a phosphonofluoridate inhibitor
Structural highlights
FunctionGLPG_ECOLI Rhomboid-type serine protease that catalyzes intramembrane proteolysis.[1] [2] Publication Abstract from PubMedRhomboid protease conducts proteolysis inside the hydrophobic environment of the membrane. The conformational flexibility of the protease is essential for the enzyme mechanism, but the nature of this flexibility is not completely understood. Here we describe the crystal structure of rhomboid protease GlpG in complex with a phosphonofluoridate inhibitor, which is covalently bonded to the catalytic serine and extends into the S' side of the substrate binding cleft. Inhibitor binding causes subtle but extensive changes in the membrane protease. Many transmembrane helices tilt and shift positions, and the gap between S2 and S5 is slightly widened so that the inhibitor can bind between them. The side chain of Phe-245 from a loop (L5) that acts as a cap rotates and uncovers the opening of the substrate binding cleft to the lipid bilayer. A concurrent turn of the polypeptide backbone at Phe-245 moves the rest of the cap and exposes the catalytic serine to the aqueous solution. This study, together with earlier crystallographic investigation of smaller inhibitors, suggests a simple model for explaining substrate binding to rhomboid protease. Conformational Change in Rhomboid Protease GlpG Induced by Inhibitor Binding to Its S' Subsites.,Xue Y, Chowdhury S, Liu X, Akiyama Y, Ellman J, Ha Y Biochemistry. 2012 May 8;51(18):3723-31. Epub 2012 Apr 24. PMID:22515733[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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