1byj

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[[Image:1byj.jpg|left|200px]]
 
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{{Structure
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==GENTAMICIN C1A A-SITE COMPLEX==
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|PDB= 1byj |SIZE=350|CAPTION= <scene name='initialview01'>1byj</scene>
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<StructureSection load='1byj' size='340' side='right'caption='[[1byj]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=GE1:3,4-DIDEOXY-2,6-AMINO-ALPHA-D+GALACTOPYRANOSE'>GE1</scene>, <scene name='pdbligand=GE2:3,5-DIAMINO-CYCLOHEXANOL'>GE2</scene>, <scene name='pdbligand=GE3:5-METHYL-4-METHYLAMINO-TETRAHYDRO-PYRAN-2,3,5-TRIOL'>GE3</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
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<table><tr><td colspan='2'>[[1byj]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BYJ FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GE1:3,4-DIDEOXY-2,6-AMINO-ALPHA-D+GALACTOPYRANOSE'>GE1</scene>, <scene name='pdbligand=GE2:3,5-DIAMINO-CYCLOHEXANOL'>GE2</scene>, <scene name='pdbligand=GE3:5-METHYL-4-METHYLAMINO-TETRAHYDRO-PYRAN-2,3,5-TRIOL'>GE3</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1byj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byj OCA], [https://pdbe.org/1byj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1byj RCSB], [https://www.ebi.ac.uk/pdbsum/1byj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1byj ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1byj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byj OCA], [http://www.ebi.ac.uk/pdbsum/1byj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1byj RCSB]</span>
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<div style="background-color:#fffaf0;">
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}}
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== Publication Abstract from PubMed ==
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'''GENTAMICIN C1A A-SITE COMPLEX'''
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==Overview==
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Aminoglycoside antibiotics that bind to the ribosomal A site cause misreading of the genetic code and inhibit translocation. The clinically important aminoglycoside, gentamicin C, is a mixture of three components. Binding of each gentamicin component to the ribosome and to a model RNA oligonucleotide was studied biochemically and the structure of the RNA complexed to gentamicin C1a was solved using magnetic resonance nuclear spectroscopy. Gentamicin C1a binds in the major groove of the RNA. Rings I and II of gentamicin direct specific RNA-drug interactions. Ring III of gentamicin, which distinguishes this subclass of aminoglycosides, also directs specific RNA interactions with conserved base pairs. The structure leads to a general model for specific ribosome recognition by aminoglycoside antibiotics and a possible mechanism for translational inhibition and miscoding. This study provides a structural rationale for chemical synthesis of novel aminoglycosides.
Aminoglycoside antibiotics that bind to the ribosomal A site cause misreading of the genetic code and inhibit translocation. The clinically important aminoglycoside, gentamicin C, is a mixture of three components. Binding of each gentamicin component to the ribosome and to a model RNA oligonucleotide was studied biochemically and the structure of the RNA complexed to gentamicin C1a was solved using magnetic resonance nuclear spectroscopy. Gentamicin C1a binds in the major groove of the RNA. Rings I and II of gentamicin direct specific RNA-drug interactions. Ring III of gentamicin, which distinguishes this subclass of aminoglycosides, also directs specific RNA interactions with conserved base pairs. The structure leads to a general model for specific ribosome recognition by aminoglycoside antibiotics and a possible mechanism for translational inhibition and miscoding. This study provides a structural rationale for chemical synthesis of novel aminoglycosides.
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==About this Structure==
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Structural origins of gentamicin antibiotic action.,Yoshizawa S, Fourmy D, Puglisi JD EMBO J. 1998 Nov 16;17(22):6437-48. PMID:9822590<ref>PMID:9822590</ref>
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1BYJ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYJ OCA].
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==Reference==
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Structural origins of gentamicin antibiotic action., Yoshizawa S, Fourmy D, Puglisi JD, EMBO J. 1998 Nov 16;17(22):6437-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9822590 9822590]
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[[Category: Protein complex]]
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[[Category: Fourmy, D.]]
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[[Category: Puglisi, J D.]]
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[[Category: Yoshizawa, S.]]
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[[Category: complex (aminoglycoside/ribosomal rna)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:10:55 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1byj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Fourmy D]]
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[[Category: Puglisi JD]]
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[[Category: Yoshizawa S]]

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GENTAMICIN C1A A-SITE COMPLEX

PDB ID 1byj

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