4xwu

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'''Unreleased structure'''
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==Structure of the IMP dehydrogenase from Ashbya gossypii==
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<StructureSection load='4xwu' size='340' side='right' caption='[[4xwu]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4xwu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XWU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XWU FirstGlance]. <br>
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</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=4xwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xwu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xwu RCSB], [http://www.ebi.ac.uk/pdbsum/4xwu PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/Q756Z6_ASHGO Q756Z6_ASHGO]] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.[HAMAP-Rule:MF_03156]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Guanine nucleotides are the precursors of essential biomolecules including nucleic acids and vitamins such as riboflavin. The enzyme inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the ratelimiting step in the guanine nucleotide de novo biosynthetic pathway and plays a key role in controlling the cellular nucleotide pools. Thus, IMPDH is an important metabolic bottleneck in the guanine nucleotide synthesis, susceptible of manipulation by means of metabolic engineering approaches. Herein, we report the functional and structural characterization of the IMPDH enzyme from the industrial fungus Ashbya gossypii. Our data show that the overexpression of the IMPDH gene increases the metabolic flux through the guanine pathway and ultimately enhances 40 % riboflavin production with respect to the wild type. Also, IMPDH disruption results in a 100-fold increase of inosine excretion to the culture media. Our results contribute to the developing metabolic engineering toolbox aiming at improving the production of metabolites with biotechnological interest in A. gossypii.
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The entry 4xwu is ON HOLD until Paper Publication
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Increased riboflavin production by manipulation of inosine 5'-monophosphate dehydrogenase in Ashbya gossypii.,Buey RM, Ledesma-Amaro R, Balsera M, de Pereda JM, Revuelta JL Appl Microbiol Biotechnol. 2015 Jul 7. PMID:26150243<ref>PMID:26150243</ref>
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Authors: Buey, R.M., Ledesma-Amaro, R., Balsera, M., de Pereda, J.M., Revuelta, J.L.
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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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Description: Structure of the IMP dehydrogenase from Ashbya gossypii
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: De Pereda, J.M]]
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__TOC__
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[[Category: Revuelta, J.L]]
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</StructureSection>
[[Category: Balsera, M]]
[[Category: Balsera, M]]
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[[Category: Buey, R M]]
[[Category: Ledesma-Amaro, R]]
[[Category: Ledesma-Amaro, R]]
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[[Category: Buey, R.M]]
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[[Category: Pereda, J M.de]]
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[[Category: Revuelta, J L]]
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[[Category: Ashbya gossypii]]
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[[Category: Imp dehydrogenase]]
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[[Category: Oxidoreductase]]

Revision as of 14:07, 22 July 2015

Structure of the IMP dehydrogenase from Ashbya gossypii

4xwu, resolution 1.75Å

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