7u3b

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Current revision (10:02, 25 December 2024) (edit) (undo)
 
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/A0A5P2ALW6_STRVZ A0A5P2ALW6_STRVZ]
[https://www.uniprot.org/uniprot/A0A5P2ALW6_STRVZ A0A5P2ALW6_STRVZ]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Streptomyces are our principal source of antibiotics, which they generate concomitant with a complex developmental transition from vegetative hyphae to spores. c-di-GMP acts as a linchpin in this transition by binding and regulating the key developmental regulators, BldD and WhiG. Here we show that c-di-GMP also binds the glycogen-debranching-enzyme, GlgX, uncovering a direct link between c-di-GMP and glycogen metabolism in bacteria. Further, we show c-di-GMP binding is required for GlgX activity. We describe structures of apo and c-di-GMP-bound GlgX and, strikingly, their comparison shows c-di-GMP induces long-range conformational changes, reorganizing the catalytic pocket to an active state. Glycogen is an important glucose storage compound that enables animals to cope with starvation and stress. Our in vivo studies reveal the important biological role of GlgX in Streptomyces glucose availability control. Overall, we identify a function of c-di-GMP in controlling energy storage metabolism in bacteria, which is widespread in Actinobacteria.
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Allosteric regulation of glycogen breakdown by the second messenger cyclic di-GMP.,Schumacher MA, Wormann ME, Henderson M, Salinas R, Latoscha A, Al-Bassam MM, Singh KS, Barclay E, Gunka K, Tschowri N Nat Commun. 2022 Oct 3;13(1):5834. doi: 10.1038/s41467-022-33537-w. PMID:36192422<ref>PMID:36192422</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 class="pdbe-citations 7u3b" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
</StructureSection>
</StructureSection>

Current revision

Structure of S. venezuelae GlgX bound to c-di-GMP and acarbose (pH 8.5)

PDB ID 7u3b

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