3f7o: Difference between revisions
New page: '''Unreleased structure''' The entry 3f7o is ON HOLD Authors: Liang, Lianming, Lou, Zhiyong, Meng, Zhaohui, Rao, Zihe, Zhang, Keqin Description: crystal structure of Cuticle-Degrading ... |
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==Crystal structure of Cuticle-Degrading Protease from Paecilomyces lilacinus (PL646)== | |||
<StructureSection load='3f7o' size='340' side='right'caption='[[3f7o]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3f7o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Purpureocillium_lilacinum Purpureocillium lilacinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F7O 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]] 2.2Å</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>, <scene name='pdbligand=HMB:(4S)-4-HYDROXY-4-METHOXYBUTANOIC+ACID'>HMB</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=3f7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f7o OCA], [https://pdbe.org/3f7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f7o RCSB], [https://www.ebi.ac.uk/pdbsum/3f7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f7o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q01471_PURLI Q01471_PURLI] | |||
== 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/f7/3f7o_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3f7o ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cuticle-degrading proteases are involved in the breakdown of cuticle/eggshells of nematodes or insects, a hard physical barrier against fungal infections. Understanding the 3-dimensional structures of these proteins can provide crucial information for improving the effectiveness of these fungi in biocontrol applications, e.g., by targeted protein engineering. However, the structures of these proteases remain unknown. Here, we report the structures of two cuticle-degrading proteases from two species of nematophagous fungi. The two structures were solved with X-ray crystallography to resolutions of 1.65 A (Ver112) and 2.1 A (PL646), respectively. Crystal structures of PL646 and Ver112 were found to be very similar to each other, and similar to that of proteinase K from another fungus Tritirachium album. Differences between the structures were found among residues of the substrate binding sites (S1 and S4). Experimental studies showed that the enzymes differed in hydrolytic activity to synthetic peptide substrates. Our analyses of the hydrophobic/hydrophilic and electrostatic features of these two proteins suggest that their surfaces likely play important roles during fungal infection against nematodes. The two crystal structures provide a solid basis for investigating the relationship between structure and function of cuticle-degrading proteases. | |||
The crystal structures of two cuticle-degrading proteases from nematophagous fungi and their contribution to infection against nematodes.,Liang L, Meng Z, Ye F, Yang J, Liu S, Sun Y, Guo Y, Mi Q, Huang X, Zou C, Rao Z, Lou Z, Zhang KQ FASEB J. 2010 May;24(5):1391-400. doi: 10.1096/fj.09-136408. Epub 2009 Dec 9. PMID:20007510<ref>PMID:20007510</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3f7o" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Purpureocillium lilacinum]] | |||
[[Category: Liang L]] | |||
[[Category: Lou Z]] | |||
[[Category: Meng Z]] | |||
[[Category: Rao Z]] | |||
[[Category: Zhang K]] | |||
Latest revision as of 18:27, 1 November 2023
Crystal structure of Cuticle-Degrading Protease from Paecilomyces lilacinus (PL646)Crystal structure of Cuticle-Degrading Protease from Paecilomyces lilacinus (PL646)
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCuticle-degrading proteases are involved in the breakdown of cuticle/eggshells of nematodes or insects, a hard physical barrier against fungal infections. Understanding the 3-dimensional structures of these proteins can provide crucial information for improving the effectiveness of these fungi in biocontrol applications, e.g., by targeted protein engineering. However, the structures of these proteases remain unknown. Here, we report the structures of two cuticle-degrading proteases from two species of nematophagous fungi. The two structures were solved with X-ray crystallography to resolutions of 1.65 A (Ver112) and 2.1 A (PL646), respectively. Crystal structures of PL646 and Ver112 were found to be very similar to each other, and similar to that of proteinase K from another fungus Tritirachium album. Differences between the structures were found among residues of the substrate binding sites (S1 and S4). Experimental studies showed that the enzymes differed in hydrolytic activity to synthetic peptide substrates. Our analyses of the hydrophobic/hydrophilic and electrostatic features of these two proteins suggest that their surfaces likely play important roles during fungal infection against nematodes. The two crystal structures provide a solid basis for investigating the relationship between structure and function of cuticle-degrading proteases. The crystal structures of two cuticle-degrading proteases from nematophagous fungi and their contribution to infection against nematodes.,Liang L, Meng Z, Ye F, Yang J, Liu S, Sun Y, Guo Y, Mi Q, Huang X, Zou C, Rao Z, Lou Z, Zhang KQ FASEB J. 2010 May;24(5):1391-400. doi: 10.1096/fj.09-136408. Epub 2009 Dec 9. PMID:20007510[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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