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3odj

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Current revision (10:34, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3odj' size='340' side='right'caption='[[3odj]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
<StructureSection load='3odj' size='340' side='right'caption='[[3odj]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3odj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ODJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ODJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3odj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ODJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ODJ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2nr9|2nr9]], [[3b44|3b44]], [[3b45|3b45]], [[2o7l|2o7l]], [[2nrf|2nrf]], [[2irv|2irv]], [[2ic8|2ic8]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glpG, HI_0618 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Rhomboid_protease Rhomboid protease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.105 3.4.21.105] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3odj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odj OCA], [https://pdbe.org/3odj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3odj RCSB], [https://www.ebi.ac.uk/pdbsum/3odj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3odj ProSAT]</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=3odj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odj OCA], [https://pdbe.org/3odj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3odj RCSB], [https://www.ebi.ac.uk/pdbsum/3odj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3odj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GLPG_HAEIN GLPG_HAEIN]] Rhomboid-type serine protease that catalyzes intramembrane proteolysis (By similarity).
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[https://www.uniprot.org/uniprot/GLPG_HAEIN GLPG_HAEIN] Rhomboid-type serine protease that catalyzes intramembrane proteolysis (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rhomboids are a remarkable class of serine proteases that are embedded in lipid membranes. These membrane-bound enzymes play key roles in cellular signaling events, and disruptions in these events can result in numerous disease pathologies, including hereditary blindness, type 2 diabetes, Parkinson's disease, and epithelial cancers. Recent crystal structures of rhomboids from Escherichia coli have focused on how membrane-bound substrates gain access to a buried active site. In E. coli, it has been shown that movements of loop 5, with smaller movements in helix 5 and loop 4, act as substrate gate, facilitating inhibitor access to rhomboid catalytic residues. Herein we present a new structure of the Haemophilus influenzae rhomboid hiGlpG, which reveals disorder in loop 5, helix 5, and loop 4, indicating that, together, they represent mobile elements of the substrate gate. Substrate cleavage assays by hiGlpG with amino acid substitutions in these mobile regions demonstrate that the flexibilities of both loop 5 and helix 5 are important for access of the substrates to the catalytic residues. Mutagenesis indicates that less mobility by loop 4 is required for substrate cleavage. A reexamination of the reaction mechanism of rhomboid substrates, whereby cleavage of the scissile bond occurs on the si-face of the peptide bond, is discussed.
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Insights into Substrate Gating in H. influenzae Rhomboid.,Brooks CL, Lazareno-Saez C, Lamoureux JS, Mak MW, Lemieux MJ J Mol Biol. 2011 Feb 3. PMID:21295583<ref>PMID:21295583</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3odj" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Rhomboid protease|Rhomboid protease]]
*[[Rhomboid protease|Rhomboid protease]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacterium influenzae lehmann and neumann 1896]]
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[[Category: Haemophilus influenzae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Rhomboid protease]]
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[[Category: Brooks CL]]
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[[Category: Brooks, C L]]
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[[Category: Lamoureux JS]]
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[[Category: Lamoureux, J S]]
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[[Category: Lazareno-Saez C]]
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[[Category: Lazareno-Saez, C]]
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[[Category: Lemieux MJ]]
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[[Category: Lemieux, M J]]
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[[Category: Mak MW]]
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[[Category: Mak, M W]]
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[[Category: Hydrolase]]
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[[Category: Membrane protein]]
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[[Category: Rhomboid peptidase]]
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Current revision

Crystal structure of H. influenzae rhomboid GlpG with disordered loop 4, helix 5 and loop 5

PDB ID 3odj

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