3vk5

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/A0A011_STRVD A0A011_STRVD]
[https://www.uniprot.org/uniprot/A0A011_STRVD A0A011_STRVD]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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New antibiotics are needed because of the increasing occurrence of multidrug resistance, as seen in Staphylococcus aureus (MRSA). The initiating step of the biosynthesis of the next-generation drug moenomycin is catalyzed by MoeO5, which is a prenyltransferase with triose-phosphate-isomerase barrel structure as was shown by E. Oldfield, R.-T. Guo, and co-workers in their Communication (DOI:10.1002/anie.201108002). The transferred farnesyl group undergoes a trans-to-cis conversion in its first double bond.
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Insights into the Mechanism of the Antibiotic-Synthesizing Enzyme MoeO5 from Crystal Structures of Different Complexes.,Ren F, Ko TP, Feng X, Huang CH, Chan HC, Hu Y, Wang K, Ma Y, Liang PH, Wang AH, Oldfield E, Guo RT Angew Chem Int Ed Engl. 2012 Mar 20. doi: 10.1002/anie.201201339. PMID:022434765<ref>PMID:022434765</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 3vk5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of MoeO5 in complex with its product FPG

PDB ID 3vk5

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