View source for 3zot


==Structure of E.coli rhomboid protease GlpG in complex with monobactam L29 (data set 2)==
<StructureSection load='3zot' size='340' side='right'caption='[[3zot]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zot]] 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=3ZOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZOT FirstGlance]. <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]] 2.399&#8491;</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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=L6C:PHENYL+N-[(1R)-3-OXIDANYLIDENE-1-PHENYL-PROPYL]CARBAMATE'>L6C</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=3zot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zot OCA], [https://pdbe.org/3zot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zot RCSB], [https://www.ebi.ac.uk/pdbsum/3zot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zot ProSAT]</span></td></tr>
</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;">
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zot" style="background-color:#fffaf0;"></div>

==See Also==
*[[Rhomboid protease|Rhomboid protease]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Freeman M]]
[[Category: Large JM]]
[[Category: Pierrat OA]]
[[Category: Vinothkumar KR]]