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5txe
From Proteopedia
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==AtxE2 Isopeptidase - S527A Variant with Astexin3-dC4 Bound== | ==AtxE2 Isopeptidase - S527A Variant with Astexin3-dC4 Bound== | ||
| - | <StructureSection load='5txe' size='340' side='right' caption='[[5txe]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='5txe' size='340' side='right'caption='[[5txe]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5txe]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TXE OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5txe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Asticcacaulis_excentricus_CB_48 Asticcacaulis excentricus CB 48]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TXE FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5txe OCA], [https://pdbe.org/5txe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5txe RCSB], [https://www.ebi.ac.uk/pdbsum/5txe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5txe ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ATXE2_ASTEC ATXE2_ASTEC] Lasso peptide isopeptidase that specifically hydrolyzes Astexin-2 and Astexin-3, converting them to linear peptides (PubMed:23862624). Has only a few specific contacts with subrates, because it recognizes Astexin knotted structure (principally the loop structure) (PubMed:26534965, PubMed:27998080). Its binding to lasso peptides opens them to expose the isopeptide bonds for hydrolysis (PubMed:27998080).<ref>PMID:23862624</ref> <ref>PMID:26534965</ref> <ref>PMID:27998080</ref> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Asticcacaulis excentricus CB 48]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Chekan JR]] |
| - | [[Category: | + | [[Category: Nair SK]] |
| - | + | ||
| - | + | ||
Current revision
AtxE2 Isopeptidase - S527A Variant with Astexin3-dC4 Bound
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