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| | ==Solution structure of a self-sacrificing resistance protein, CalC from Micromonospora echinospora== | | ==Solution structure of a self-sacrificing resistance protein, CalC from Micromonospora echinospora== |
| - | <StructureSection load='1zxf' size='340' side='right' caption='[[1zxf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1zxf' size='340' side='right'caption='[[1zxf]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zxf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_15837 Atcc 15837]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZXF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zxf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_echinospora Micromonospora echinospora]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZXF FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CalC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1877 ATCC 15837])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1zxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxf OCA], [http://pdbe.org/1zxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zxf RCSB], [http://www.ebi.ac.uk/pdbsum/1zxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zxf ProSAT], [http://www.topsan.org/Proteins/CESG/1zxf TOPSAN]</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=1zxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxf OCA], [https://pdbe.org/1zxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zxf RCSB], [https://www.ebi.ac.uk/pdbsum/1zxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zxf ProSAT], [https://www.topsan.org/Proteins/CESG/1zxf TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8KNF0_MICEC Q8KNF0_MICEC] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 15837]] | + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | + | [[Category: Micromonospora echinospora]] |
| - | [[Category: Griffith, B R]] | + | [[Category: Griffith BR]] |
| - | [[Category: Hager, M H]] | + | [[Category: Hager MH]] |
| - | [[Category: Hallenga, K]] | + | [[Category: Hallenga K]] |
| - | [[Category: Lee, M S]] | + | [[Category: Lee MS]] |
| - | [[Category: Markley, J L]] | + | [[Category: Markley JL]] |
| - | [[Category: Singh, S]] | + | [[Category: Singh S]] |
| - | [[Category: Thorson, J S]] | + | [[Category: Thorson JS]] |
| - | [[Category: Zhang, C]] | + | [[Category: Zhang C]] |
| - | [[Category: Cesg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Self-sacrificing resistance protein]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
Q8KNF0_MICEC
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The recent discovery of the first "self-sacrifice" mechanism for bacterial resistance to the enediyne antitumor antibiotics, where enediyne-induced proteolysis of the resistance protein CalC inactivates both the highly reactive metabolite and the resistance protein, revealed yet another ingenious bacterial mechanism for controlling reactive metabolites. As reported herein, the first 3D structures of CalC and CalC in complex with calicheamicin (CLM) divulge CalC to be a member of the steroidogenic acute regulatory protein (StAR)-related transfer (START) domain superfamily. In contrast to previous studies of proteins known to bind DNA-damaging natural products ( e.g ., bleomycins, mitomycins, and nine-membered chromoprotein enediynes), this is the first demonstrated involvement of a START domain fold. Consistent with the CalC self-sacrifice mechanism, CLM in complex with CalC is positioned for direct hydrogen abstraction from Gly113 to initiate the oxidative proteolysis-based resistance mechanism. These structural studies also illuminate, for the first time, a small DNA-binding region within CalC that may serve to localize CalC to the enediyne target (DNA). Given the role of START domains in nuclear/cytosolic transport and translocation, this structural study also may implicate START domains as post-endocytotic intracellular chaperones for enediyne-based therapeutics such as MyloTarg.
Structural insight into the self-sacrifice mechanism of enediyne resistance.,Singh S, Hager MH, Zhang C, Griffith BR, Lee MS, Hallenga K, Markley JL, Thorson JS ACS Chem Biol. 2006 Aug 22;1(7):451-60. PMID:17168523[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Singh S, Hager MH, Zhang C, Griffith BR, Lee MS, Hallenga K, Markley JL, Thorson JS. Structural insight into the self-sacrifice mechanism of enediyne resistance. ACS Chem Biol. 2006 Aug 22;1(7):451-60. PMID:17168523 doi:10.1021/cb6002898
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