|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5d7w' size='340' side='right'caption='[[5d7w]], [[Resolution|resolution]] 1.10Å' scene=''> | | <StructureSection load='5d7w' size='340' side='right'caption='[[5d7w]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5d7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_marcescens"_(bizio_1823)_trevisan_in_de_toni_and_trevisan_1889 "bacillus marcescens" (bizio 1823) trevisan in de toni and trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D7W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5d7w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D7W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40] </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=5d7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d7w OCA], [https://pdbe.org/5d7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d7w RCSB], [https://www.ebi.ac.uk/pdbsum/5d7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d7w 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=5d7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d7w OCA], [http://pdbe.org/5d7w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d7w RCSB], [http://www.ebi.ac.uk/pdbsum/5d7w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d7w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRZN_SERMA PRZN_SERMA]] Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death. | + | [https://www.uniprot.org/uniprot/PRZN_SERMA PRZN_SERMA] Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Serralysin]] | + | [[Category: Serratia marcescens]] |
| - | [[Category: Ran, T]] | + | [[Category: Ran T]] |
| - | [[Category: Wang, W]] | + | [[Category: Wang W]] |
| - | [[Category: Wu, D]] | + | [[Category: Wu D]] |
| - | [[Category: Xu, D Q]] | + | [[Category: Xu DQ]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metalloprotease]]
| + | |
| - | [[Category: Protease]]
| + | |
| Structural highlights
Function
PRZN_SERMA Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death.
Publication Abstract from PubMed
Serralysin is a well studied metalloprotease, and typical serralysins are not thermostable. The serralysin isolated from Serratia sp. FS14 was found to be thermostable, and in order to reveal the mechanism responsible for its thermostability, the crystal structure of serralysin from Serratia sp. FS14 was solved to a crystallographic R factor of 0.1619 at 1.10 A resolution. Similar to its homologues, it mainly consists of two domains: an N-terminal catalytic domain and a `parallel beta-roll' C-terminal domain. Comparative studies show that the shape of the catalytic active-site cavity is more open owing to the 189-198 loop, with a short 310-helix protruding further from the molecular surface, and that the beta-sheets comprising the `parallel beta-roll' are longer than those in its homologues. The formation of hydrogen bonds from one of the nonconserved residues (Asn200) to Lys27 may contribute to the thermostability.
Structure of a thermostable serralysin from Serratia sp. FS14 at 1.1 A resolution.,Wu D, Ran T, Wang W, Xu D Acta Crystallogr F Struct Biol Commun. 2016 Jan;72(Pt 1):10-5. doi:, 10.1107/S2053230X15023092. Epub 2016 Jan 1. PMID:26750478[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wu D, Ran T, Wang W, Xu D. Structure of a thermostable serralysin from Serratia sp. FS14 at 1.1 A resolution. Acta Crystallogr F Struct Biol Commun. 2016 Jan;72(Pt 1):10-5. doi:, 10.1107/S2053230X15023092. Epub 2016 Jan 1. PMID:26750478 doi:http://dx.doi.org/10.1107/S2053230X15023092
|
