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4q85

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<StructureSection load='4q85' size='340' side='right'caption='[[4q85]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
<StructureSection load='4q85' size='340' side='right'caption='[[4q85]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4q85]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q85 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4q85]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q85 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.29&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q84|4q84]], [[4q86|4q86]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ycaO, b0905, JW0888 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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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=4q85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q85 OCA], [https://pdbe.org/4q85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q85 RCSB], [https://www.ebi.ac.uk/pdbsum/4q85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q85 ProSAT]</span></td></tr>
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<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=4q85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q85 OCA], [http://pdbe.org/4q85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q85 RCSB], [http://www.ebi.ac.uk/pdbsum/4q85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q85 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/YCAO_ECOLI YCAO_ECOLI]] Involved in beta-methylthiolation of ribosomal protein S12.
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[https://www.uniprot.org/uniprot/YCAO_ECOLI YCAO_ECOLI] Involved in beta-methylthiolation of ribosomal protein S12.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Despite intensive research, the cyclodehydratase responsible for azoline biogenesis in thiazole/oxazole-modified microcin (TOMM) natural products remains enigmatic. The collaboration of two proteins, C and D, is required for cyclodehydration. The C protein is homologous to E1 ubiquitin-activating enzymes, whereas the D protein is within the YcaO superfamily. Recent studies have demonstrated that TOMM YcaOs phosphorylate amide carbonyl oxygens to facilitate azoline formation. Here we report the X-ray crystal structure of an uncharacterized YcaO from Escherichia coli (Ec-YcaO). Ec-YcaO harbors an unprecedented fold and ATP-binding motif. This motif is conserved among TOMM YcaOs and is required for cyclodehydration. Furthermore, we demonstrate that the C protein regulates substrate binding and catalysis and that the proline-rich C terminus of the D protein is involved in C protein recognition and catalysis. This study identifies the YcaO active site and paves the way for the characterization of the numerous YcaO domains not associated with TOMM biosynthesis.
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Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.,Dunbar KL, Chekan JR, Cox CL, Burkhart BJ, Nair SK, Mitchell DA Nat Chem Biol. 2014 Aug 17. doi: 10.1038/nchembio.1608. PMID:25129028<ref>PMID:25129028</ref>
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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 4q85" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chekan, J R]]
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[[Category: Chekan JR]]
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[[Category: Nair, S K]]
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[[Category: Nair SK]]
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[[Category: Protein binding]]
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[[Category: Ycao atp binding domain]]
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Current revision

YcaO with Non-hydrolyzable ATP (AMPCPP) Bound

PDB ID 4q85

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