2xxl: Difference between revisions
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<StructureSection load='2xxl' size='340' side='right'caption='[[2xxl]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2xxl' size='340' side='right'caption='[[2xxl]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xxl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2xxl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XXL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2xxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxl OCA], [https://pdbe.org/2xxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xxl RCSB], [https://www.ebi.ac.uk/pdbsum/2xxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xxl 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=2xxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxl OCA], [https://pdbe.org/2xxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xxl RCSB], [https://www.ebi.ac.uk/pdbsum/2xxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xxl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GRASS_DROME GRASS_DROME] Endopeptidase (By similarity). Plays a key role in innate immunity by activating the Toll pathway in response to fungal and Gram-positive bacterial infections, presumably downstream of pattern-recognition receptors (PRR), such as PGRP-SA, GNBP1 and GNBP3, and upstream of spz processing enzyme SPE (PubMed:16631589, PubMed:18724373).[UniProtKB:Q9XXV0]<ref>PMID:16631589</ref> <ref>PMID:18724373</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: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Coquet L]] | |||
[[Category: Coquet | [[Category: Jouenne T]] | ||
[[Category: Jouenne | [[Category: Kellenberger C]] | ||
[[Category: Kellenberger | [[Category: Leone P]] | ||
[[Category: Leone | [[Category: Reichhart JM]] | ||
[[Category: Reichhart | [[Category: Roussel A]] | ||
[[Category: Roussel | |||
Latest revision as of 13:40, 20 December 2023
Crystal structure of drosophila Grass clip serine protease of Toll pathwayCrystal structure of drosophila Grass clip serine protease of Toll pathway
Structural highlights
FunctionGRASS_DROME Endopeptidase (By similarity). Plays a key role in innate immunity by activating the Toll pathway in response to fungal and Gram-positive bacterial infections, presumably downstream of pattern-recognition receptors (PRR), such as PGRP-SA, GNBP1 and GNBP3, and upstream of spz processing enzyme SPE (PubMed:16631589, PubMed:18724373).[UniProtKB:Q9XXV0][1] [2] Publication Abstract from PubMedGrass is a clip domain serine protease (SP) involved in a proteolytic cascade triggering the Toll pathway activation of Drosophila during an immune response. Epistasic studies position it downstream of the apical protease ModSP and upstream of the terminal protease Spaetzle-processing enzyme. Here, we report the crystal structure of Grass zymogen. We found that Grass displays a rather deep active site cleft comparable with that of proteases of coagulation and complement cascades. A key distinctive feature is the presence of an additional loop (75-loop) in the proximity of the activation site localized on a protruding loop. All biochemical attempts to hydrolyze the activation site of Grass failed, strongly suggesting restricted access to this region. The 75-loop is thus proposed to constitute an original mechanism to prevent spontaneous activation. A comparison of Grass with clip serine proteases of known function involved in analogous proteolytic cascades allowed us to define two groups, according to the presence of the 75-loop and the conformation of the clip domain. One group (devoid of the 75-loop) contains penultimate proteases whereas the other contains terminal proteases. Using this classification, Grass appears to be a terminal protease. This result is evaluated according to the genetic data documenting Grass function. Structure-function analysis of grass clip serine protease involved in Drosophila Toll pathway activation.,Kellenberger C, Leone P, Coquet L, Jouenne T, Reichhart JM, Roussel A J Biol Chem. 2011 Apr 8;286(14):12300-7. Epub 2011 Feb 10. PMID:21310954[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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