2xxl: Difference between revisions
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== | ==Crystal structure of drosophila Grass clip serine protease of Toll pathway== | ||
<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 [http://en.wikipedia.org/wiki/Drome Drome]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XXL FirstGlance]. <br> | <table><tr><td colspan='2'>[[2xxl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XXL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </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=2xxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxl OCA], [http://pdbe.org/2xxl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xxl RCSB], [http://www.ebi.ac.uk/pdbsum/2xxl PDBsum], [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxl OCA], [http://pdbe.org/2xxl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xxl RCSB], [http://www.ebi.ac.uk/pdbsum/2xxl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xxl ProSAT]</span></td></tr> | ||
Revision as of 12:04, 10 October 2018
Crystal structure of drosophila Grass clip serine protease of Toll pathwayCrystal structure of drosophila Grass clip serine protease of Toll pathway
Structural highlights
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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