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==Structure of E.coli rhomboid protease GlpG in complex with monobactam L62== | |||
<StructureSection load='3zmh' size='340' side='right' caption='[[3zmh]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zmh]] 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=3ZMH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZMH FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=78C:CYCLOPENTYL+2-OXO-4-PHENYLAZETIDINE-1-CARBOXYLATE'>78C</scene>, <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=L62:CYCLOPENTYL+N-[(1R)-3-OXIDANYLIDENE-1-PHENYL-PROPYL]CARBAMATE'>L62</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zmi|3zmi]], [[3zmj|3zmj]], [[3zot|3zot]]</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=3zmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zmh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zmh RCSB], [http://www.ebi.ac.uk/pdbsum/3zmh 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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rhomboids are evolutionarily conserved serine proteases that cleave transmembrane proteins within the membrane. The increasing number of known rhomboid functions in prokaryotes and eukaryotes makes them attractive drug targets. Here, we describe structures of the Escherichia coli rhomboid GlpG in complex with beta-lactam inhibitors. The inhibitors form a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of beta-lactam inhibitors points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site of GlpG. We suggest that the structural changes in beta-lactam inhibitor binding reflect the state of the enzyme at an initial stage of substrate binding to the active site. The structural insights from these enzyme-inhibitor complexes provide a starting point for structure-based design for rhomboid inhibitors. | |||
Structure of Rhomboid Protease in Complex with beta-Lactam Inhibitors Defines the S2' Cavity.,Vinothkumar KR, Pierrat OA, Large JM, Freeman M Structure. 2013 May 7. pii: S0969-2126(13)00117-2. doi:, 10.1016/j.str.2013.03.013. PMID:23665170<ref>PMID:23665170</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Rhomboid protease|Rhomboid protease]] | *[[Rhomboid protease|Rhomboid protease]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Rhomboid protease]] | [[Category: Rhomboid protease]] | ||
[[Category: Freeman, M | [[Category: Freeman, M]] | ||
[[Category: Large, J M | [[Category: Large, J M]] | ||
[[Category: Pierrat, O A | [[Category: Pierrat, O A]] | ||
[[Category: Vinothkumar, K R | [[Category: Vinothkumar, K R]] | ||
[[Category: Acyl enzyme]] | [[Category: Acyl enzyme]] | ||
[[Category: Anitbiotic]] | [[Category: Anitbiotic]] | ||
Revision as of 11:52, 24 December 2014
Structure of E.coli rhomboid protease GlpG in complex with monobactam L62Structure of E.coli rhomboid protease GlpG in complex with monobactam L62
Structural highlights
Function[GLPG_ECOLI] Rhomboid-type serine protease that catalyzes intramembrane proteolysis.[1] [2] Publication Abstract from PubMedRhomboids are evolutionarily conserved serine proteases that cleave transmembrane proteins within the membrane. The increasing number of known rhomboid functions in prokaryotes and eukaryotes makes them attractive drug targets. Here, we describe structures of the Escherichia coli rhomboid GlpG in complex with beta-lactam inhibitors. The inhibitors form a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of beta-lactam inhibitors points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site of GlpG. We suggest that the structural changes in beta-lactam inhibitor binding reflect the state of the enzyme at an initial stage of substrate binding to the active site. The structural insights from these enzyme-inhibitor complexes provide a starting point for structure-based design for rhomboid inhibitors. Structure of Rhomboid Protease in Complex with beta-Lactam Inhibitors Defines the S2' Cavity.,Vinothkumar KR, Pierrat OA, Large JM, Freeman M Structure. 2013 May 7. pii: S0969-2126(13)00117-2. doi:, 10.1016/j.str.2013.03.013. PMID:23665170[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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