|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==SOLUTION STRUCTURES OF C-1027 APOPROTEIN AND ITS COMPLEX WITH THE AROMATIZED CHROMOPHORE== | | ==SOLUTION STRUCTURES OF C-1027 APOPROTEIN AND ITS COMPLEX WITH THE AROMATIZED CHROMOPHORE== |
| - | <StructureSection load='1hzk' size='340' side='right' caption='[[1hzk]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1hzk' size='340' side='right'caption='[[1hzk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hzk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_globisporus Streptomyces globisporus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HZK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hzk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_globisporus Streptomyces globisporus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZK FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hzl|1hzl]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 30 models</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=1hzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzk OCA], [http://pdbe.org/1hzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hzk RCSB], [http://www.ebi.ac.uk/pdbsum/1hzk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hzk 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=1hzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzk OCA], [https://pdbe.org/1hzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hzk RCSB], [https://www.ebi.ac.uk/pdbsum/1hzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hzk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAGA_STRGL CAGA_STRGL]] Binds non-covalently to a chromophore which is the cytotoxic and mutagenic component of the antibiotic. The chromophore binds to DNA as a weak intercalator and causes single- and double-strand breaks. | + | [https://www.uniprot.org/uniprot/CAGA_STRGL CAGA_STRGL] Binds non-covalently to a chromophore which is the cytotoxic and mutagenic component of the antibiotic. The chromophore binds to DNA as a weak intercalator and causes single- and double-strand breaks. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/1hzk_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/1hzk_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| Line 32: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Streptomyces globisporus]] | | [[Category: Streptomyces globisporus]] |
| - | [[Category: Fukuda-Ishisaka, S]] | + | [[Category: Fukuda-Ishisaka S]] |
| - | [[Category: Hirama, M]] | + | [[Category: Hirama M]] |
| - | [[Category: Otani, T]] | + | [[Category: Otani T]] |
| - | [[Category: Tanaka, T]] | + | [[Category: Tanaka T]] |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Apoprotein]]
| + | |
| - | [[Category: C-1027]]
| + | |
| - | [[Category: Chromoprotein]]
| + | |
| Structural highlights
Function
CAGA_STRGL Binds non-covalently to a chromophore which is the cytotoxic and mutagenic component of the antibiotic. The chromophore binds to DNA as a weak intercalator and causes single- and double-strand breaks.
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
C-1027 is one of the most potent antitumor antibiotic chromoproteins, and is a 1:1 complex of an enediyne chromophore having DNA-cleaving ability and a carrier apoprotein. The three-dimensional solution structures of the 110 residue (10.5 kDa) C-1027 apoprotein and its complex with the aromatized chromophore have been determined separately by homonuclear two-dimensional nuclear magnetic resonance methods. The apoprotein is mainly composed of three antiparallel beta-sheets: four-stranded beta-sheet (43-45, 52-54; 30-38; 92-94; 104-106), three-stranded beta-sheet (4-6; 17-22; 61-66), and two-stranded beta-sheet (70-72; 83-85). The overall structure of the apoprotein is very similar to those of other chromoprotein apoproteins, such as neocarzinostatin and kedarcidin. A hydrophobic pocket with approximate dimensions of 14 A x 12 A x 8 A is formed by the four-stranded beta-sheet and the three loops (39-42; 75-79; 97-100). The holoprotein (complex form with the aromatized chromophore) structure reveals that the aromatized chromophore is bound to the hydrophobic pocket found in the apoprotein. The benzodihydropentalene core of the chromophore is located in the center of the pocket and other substituents (beta-tyrosine, benzoxazine, and aminosugar moieties) are arranged around the core. Major binding interactions between the apoprotein and the chromophore are likely the hydrophobic contacts between the core of the chromophore and the hydrophobic side-chains of the pocket-forming residues, which is supplemented by salt bridges and/or hydrogen bonds. Based on the holoprotein structure, we propose possible mechanisms for the stabilization and the release of chromophore by the apoprotein.
Solution structures of C-1027 apoprotein and its complex with the aromatized chromophore.,Tanaka T, Fukuda-Ishisaka S, Hirama M, Otani T J Mol Biol. 2001 May 25;309(1):267-83. PMID:11491295[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tanaka T, Fukuda-Ishisaka S, Hirama M, Otani T. Solution structures of C-1027 apoprotein and its complex with the aromatized chromophore. J Mol Biol. 2001 May 25;309(1):267-83. PMID:11491295 doi:10.1006/jmbi.2001.4621
|
