1oyv: Difference between revisions
New page: left|200px<br /><applet load="1oyv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oyv, resolution 2.5Å" /> '''Crystal structure of ... |
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== | ==Crystal structure of tomato inhibitor-II in a ternary complex with subtilisin Carlsberg== | ||
Multidomain proteinase inhibitors play critical roles in the defense of | <StructureSection load='1oyv' size='340' side='right'caption='[[1oyv]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1oyv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [https://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OYV 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]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1oyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oyv OCA], [https://pdbe.org/1oyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oyv RCSB], [https://www.ebi.ac.uk/pdbsum/1oyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oyv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SUBC_BACLI SUBC_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (PubMed:11109488, Ref.4). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).<ref>PMID:11109488</ref> <ref>PMID:4967581</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oy/1oyv_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oyv ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Multidomain proteinase inhibitors play critical roles in the defense of plants against predation by a wide range of pests. Despite a wealth of structural information on proteinase-single domain inhibitor interactions, the structural basis of inhibition by multidomain proteinase inhibitors remains poorly understood. Here we report the 2.5-A resolution crystal structure of the two-headed tomato inhibitor-II (TI-II) in complex with two molecules of subtilisin Carlsberg; it reveals how a multidomain inhibitor from the Potato II family of proteinase inhibitors can bind to and simultaneously inhibit two enzyme molecules within a single ternary complex. The N terminus of TI-II initiates the folding of Domain I (Lys-1 to Cys-15 and Pro-84 to Met-123) and then completes Domain II (Ile-26 to Pro-74) before coming back to complete the rest of Domain I (Pro-84 to Met-123). The two domains of TI-II adopt a similar fold and are arranged in an extended configuration that presents two reactive site loops at the opposite ends of the inhibitor molecule. Each subtilisin molecule interacts with a reactive site loop of TI-II through the standard, canonical binding mode. Remarkably, a significant distortion of the active site of subtilisin is induced by the presence of phenylalanine in the P1 position of reactive site loop II of TI-II. The structure of the TI-II.(subtilisin)2 complex provides a molecular framework for understanding how multiple inhibitory domains in a single Potato II type proteinase inhibitor molecule from the Potato II family act to inhibit proteolytic enzymes. | |||
Structural basis of inhibition revealed by a 1:2 complex of the two-headed tomato inhibitor-II and subtilisin Carlsberg.,Barrette-Ng IH, Ng KK, Cherney MM, Pearce G, Ryan CA, James MN J Biol Chem. 2003 Jun 27;278(26):24062-71. Epub 2003 Apr 8. PMID:12684499<ref>PMID:12684499</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1oyv" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Subtilisin 3D structures|Subtilisin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Solanum lycopersicum]] | [[Category: Solanum lycopersicum]] | ||
[[Category: Barrette-Ng IH]] | |||
[[Category: Barrette-Ng | [[Category: Cherney MM]] | ||
[[Category: Cherney | [[Category: James MN]] | ||
[[Category: James | [[Category: Ng KK]] | ||
[[Category: Ng | [[Category: Pearce G]] | ||
[[Category: Pearce | [[Category: Ryan CA]] | ||
[[Category: Ryan | |||
