2l65

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:53, 1 May 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==HADDOCK calculated model of the complex of the resistance protein CalC and Calicheamicin-Gamma==
==HADDOCK calculated model of the complex of the resistance protein CalC and Calicheamicin-Gamma==
-
<StructureSection load='2l65' size='340' side='right'caption='[[2l65]], [[NMR_Ensembles_of_Models | 4 NMR models]]' scene=''>
+
<StructureSection load='2l65' size='340' side='right'caption='[[2l65]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2l65]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_15835_[[micromonospora_purpurea_luedemann_and_brodsky_1964_(approved_lists_1980)]] Atcc 15835 [[micromonospora purpurea luedemann and brodsky 1964 (approved lists 1980)]]]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2gkc 2gkc]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L65 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2l65]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_echinospora Micromonospora echinospora]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2gkc 2gkc]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L65 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DSR:2,6-DIDEOXY-4-THIO-BETA-D-ALLOSEPYRANOSIDE'>DSR</scene>, <scene name='pdbligand=HIB:4-HYDROXY-5-IODO-2,3-DIMETHOXY-6-METHYLBENZOIC+ACID'>HIB</scene>, <scene name='pdbligand=MRP:3-O-METHYL-ALPHA-L-RHAMNOPYRANOSIDE'>MRP</scene>, <scene name='pdbligand=MTC:[1,8-DIHYDROXY-11-OXO-13-(2-METHYLTRITHIO-ETHYLIDENE)-BICYCLO[7.3.1]TRIDECA-4,9-DIENE-2,6-DIYN-10-YL]-CARBAMIC+ACID+METHYL+ESTER'>MTC</scene>, <scene name='pdbligand=DAG:4,6-DIDEOXY-4-AMINO-BETA-D-GLUCOPYRANOSIDE'>DAG</scene></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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=EMP:2,4-DIDEOXY-4-(ETHYLAMINO)-3-O-METHYL+ALPHA-L-THREO-PENTOPYRANOSIDE'>EMP</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAG:4,6-DIDEOXY-4-AMINO-BETA-D-GLUCOPYRANOSIDE'>DAG</scene>, <scene name='pdbligand=DSR:2,6-DIDEOXY-4-THIO-BETA-D-ALLOSEPYRANOSIDE'>DSR</scene>, <scene name='pdbligand=EMP:2,4-DIDEOXY-4-(ETHYLAMINO)-3-O-METHYL+ALPHA-L-THREO-PENTOPYRANOSIDE'>EMP</scene>, <scene name='pdbligand=HIB:4-HYDROXY-5-IODO-2,3-DIMETHOXY-6-METHYLBENZOIC+ACID'>HIB</scene>, <scene name='pdbligand=MRP:3-O-METHYL-ALPHA-L-RHAMNOPYRANOSIDE'>MRP</scene>, <scene name='pdbligand=MTC:[1,8-DIHYDROXY-11-OXO-13-(2-METHYLTRITHIO-ETHYLIDENE)-BICYCLO[7.3.1]TRIDECA-4,9-DIENE-2,6-DIYN-10-YL]-CARBAMIC+ACID+METHYL+ESTER'>MTC</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zxf|1zxf]], [[2pik|2pik]]</div></td></tr>
+
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">calC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1877 ATCC 15835 [[Micromonospora purpurea Luedemann and Brodsky 1964 (Approved Lists 1980)]]])</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=2l65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l65 OCA], [https://pdbe.org/2l65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l65 RCSB], [https://www.ebi.ac.uk/pdbsum/2l65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l65 ProSAT]</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=2l65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l65 OCA], [https://pdbe.org/2l65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l65 RCSB], [https://www.ebi.ac.uk/pdbsum/2l65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l65 ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q8KNF0_MICEC Q8KNF0_MICEC]
-
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<ref>PMID:17168523</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 2l65" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Structural genomic]]
+
[[Category: Micromonospora echinospora]]
-
[[Category: Markley, J L]]
+
[[Category: Markley JL]]
-
[[Category: Singh, S]]
+
[[Category: Singh S]]
-
[[Category: Thorson, J S]]
+
[[Category: Thorson JS]]
-
[[Category: Cesg]]
+
-
[[Category: PSI, Protein structure initiative]]
+
-
[[Category: Resistance protein]]
+
-
[[Category: Unknown function]]
+

Current revision

HADDOCK calculated model of the complex of the resistance protein CalC and Calicheamicin-Gamma

PDB ID 2l65

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l65"
Personal tools