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Oligomeric interactions maintain active-site structure in a non-cooperative enzyme family


ABSTRACT:

SUBMITTER: John Francis Hunt 

PROVIDER: EMPIAR-10872 | biostudies-other |

REPOSITORIES: biostudies-other

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Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.

Li Yaohui Y   Zhang Rongzhen R   Wang Chi C   Forouhar Farhad F   Clarke Oliver B OB   Vorobiev Sergey S   Singh Shikha S   Montelione Gaetano T GT   Szyperski Thomas T   Xu Yan Y   Hunt John F JF  

The EMBO journal 20220708 17


The evolutionary benefit accounting for widespread conservation of oligomeric structures in proteins lacking evidence of intersubunit cooperativity remains unclear. Here, crystal and cryo-EM structures, and enzymological data, demonstrate that a conserved tetramer interface maintains the active-site structure in one such class of proteins, the short-chain dehydrogenase/reductase (SDR) superfamily. Phylogenetic comparisons support a significantly longer polypeptide being required to maintain an e  ...[more]

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