Crystal structure of a putative 3-hydroxypimelyl-CoA dehydrogenase, Hcd1, from Syntrophus aciditrophicus strain SB at 1.78 Å resolution

Journal Article · Thu May 25 00:00:00 EDT 2023 · Acta Crystallographica. Section F, Structural Biology Communications

DOI:https://doi.org/10.1107/s2053230x23004399· OSTI ID:1975175

Dinh, David M. ^[1]; Thomas, Leonard M. ^[1]; Karr, Elizabeth A.  ^[1]

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1. Univ. of Oklahoma, Norman, OK (United States)

Syntrophus aciditrophicus strain SB is a model syntroph that degrades benzoate and alicyclic acids. Here, the structure of a putative 3-hydroxypimelyl-CoA dehydrogenase from S. aciditrophicus strain SB (SaHcd1) was resolved at 1.78 Å resolution. SaHcd1 contains sequence motifs and structural features that belong to the short-chain dehydrogenase/reductase (SDR) family of NADPH-dependent oxidoreductases. SaHcd1 is proposed to concomitantly reduce NAD⁺ or NADP⁺ to NADH or NADPH, respectively, while converting 3-hydroxypimelyl-CoA to 3-oxopimeyl-CoA. Further enzymatic studies are needed to confirm the function of SaHcd1.

• Research Organization: Univ. of Oklahoma, Norman, OK (United States)
• Sponsoring Organization: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH)
• Grant/Contract Number: FG02-96ER20214; AC02-76SF00515; P20GM103640; P41GM103393
• OSTI ID: 1975175
• Journal Information: Acta Crystallographica. Section F, Structural Biology Communications, Vol. 79, Issue 6; ISSN 2053-230X
• Publisher: International Union of Crystallography
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
SDR family protein
syntrophy
fatty acid metabolism
Syntrophus aciditrophicus