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==Structure of the SK/DHQase/DHSD dimer from Candida albicans Aro1== | ==Structure of the SK/DHQase/DHSD dimer from Candida albicans Aro1== | ||
<StructureSection load='7u5u' size='340' side='right'caption='[[7u5u]]' scene=''> | <StructureSection load='7u5u' size='340' side='right'caption='[[7u5u]], [[Resolution|resolution]] 3.16Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7U5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7U5U FirstGlance]. <br> | <table><tr><td colspan='2'>[[7u5u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7U5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7U5U FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7u5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7u5u OCA], [https://pdbe.org/7u5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7u5u RCSB], [https://www.ebi.ac.uk/pdbsum/7u5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7u5u ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7u5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7u5u OCA], [https://pdbe.org/7u5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7u5u RCSB], [https://www.ebi.ac.uk/pdbsum/7u5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7u5u ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/ARO1_CANAL ARO1_CANAL]] The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In the human fungal pathogen Candida albicans, ARO1 encodes an essential multi-enzyme that catalyses consecutive steps in the shikimate pathway for biosynthesis of chorismate, a precursor to folate and the aromatic amino acids. We obtained the first molecular image of C. albicans Aro1 that reveals the architecture of all five enzymatic domains and their arrangement in the context of the full-length protein. Aro1 forms a flexible dimer allowing relative autonomy of enzymatic function of the individual domains. Our activity and in cellulo data suggest that only four of Aro1's enzymatic domains are functional and essential for viability of C. albicans, whereas the 3-dehydroquinate dehydratase (DHQase) domain is inactive because of active site substitutions. We further demonstrate that in C. albicans, the type II DHQase Dqd1 can compensate for the inactive DHQase domain of Aro1, suggesting an unrecognized essential role for this enzyme in shikimate biosynthesis. In contrast, in Candida glabrata and Candida parapsilosis, which do not encode a Dqd1 homolog, Aro1 DHQase domains are enzymatically active, highlighting diversity across Candida species. | |||
Molecular analysis and essentiality of Aro1 shikimate biosynthesis multi-enzyme in Candida albicans.,Stogios PJ, Liston SD, Semper C, Quade B, Michalska K, Evdokimova E, Ram S, Otwinowski Z, Borek D, Cowen LE, Savchenko A Life Sci Alliance. 2022 May 5;5(8). pii: 5/8/e202101358. doi:, 10.26508/lsa.202101358. Print 2022 Aug. PMID:35512834<ref>PMID:35512834</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7u5u" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Candida albicans]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Borek D]] | [[Category: Borek, D]] | ||
[[Category: Otwinowski Z]] | [[Category: Otwinowski, Z]] | ||
[[Category: Quade B]] | [[Category: Quade, B]] | ||
[[Category: Biosynthetic protein]] | |||
Revision as of 13:28, 18 May 2022
Structure of the SK/DHQase/DHSD dimer from Candida albicans Aro1Structure of the SK/DHQase/DHSD dimer from Candida albicans Aro1
Structural highlights
Function[ARO1_CANAL] The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. Publication Abstract from PubMedIn the human fungal pathogen Candida albicans, ARO1 encodes an essential multi-enzyme that catalyses consecutive steps in the shikimate pathway for biosynthesis of chorismate, a precursor to folate and the aromatic amino acids. We obtained the first molecular image of C. albicans Aro1 that reveals the architecture of all five enzymatic domains and their arrangement in the context of the full-length protein. Aro1 forms a flexible dimer allowing relative autonomy of enzymatic function of the individual domains. Our activity and in cellulo data suggest that only four of Aro1's enzymatic domains are functional and essential for viability of C. albicans, whereas the 3-dehydroquinate dehydratase (DHQase) domain is inactive because of active site substitutions. We further demonstrate that in C. albicans, the type II DHQase Dqd1 can compensate for the inactive DHQase domain of Aro1, suggesting an unrecognized essential role for this enzyme in shikimate biosynthesis. In contrast, in Candida glabrata and Candida parapsilosis, which do not encode a Dqd1 homolog, Aro1 DHQase domains are enzymatically active, highlighting diversity across Candida species. Molecular analysis and essentiality of Aro1 shikimate biosynthesis multi-enzyme in Candida albicans.,Stogios PJ, Liston SD, Semper C, Quade B, Michalska K, Evdokimova E, Ram S, Otwinowski Z, Borek D, Cowen LE, Savchenko A Life Sci Alliance. 2022 May 5;5(8). pii: 5/8/e202101358. doi:, 10.26508/lsa.202101358. Print 2022 Aug. PMID:35512834[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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