6qjz

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Identificationand Characterization of an Oxalylfrom Grass pea (Lathyrus sativusCoA-Synthetase L.)

Structural highlights

6qjz is a 1 chain structure with sequence from Lathyrus sativus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:AMP
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A3G8GC37_LATSA

Publication Abstract from PubMed

Oxalic acid is a small metabolite found in many plants. It serves as protection from herbivores, a chelator of metal ions, a regulator of calcium levels, and additional tasks. However, it is also a strong di-carboxylic acid that can compromise plant viability by reducing cellular pH. Several metabolic pathways have evolved to control oxalate levels in plants by enzymatic degradation. Among them is the pathway that utilizes oxalyl-CoA synthetase (OCS, EC 6.2.1.8) and ATP to convert oxalate to oxalyl-CoA. Oxalyl-CoA can then be degraded to CO2 or utilized as a precursor for the synthesis of other compounds. In grass pea (Lathyrus sativus L.), a grain legume grown in Asia and Africa for human and animal consumption, the neurotoxic compound beta-N-oxalyl-l-alpha,beta-diaminopropionic acid (beta-ODAP) is synthesized from oxalyl-CoA and l-alpha,beta-diaminopropionic acid (l-DAPA). Here, we report on the identification and characterization of oxalyl CoA-synthetase from grass pea (LsOCS). The gene encoding LsOCS was amplified from grass pea, and then expressed and purified from E. coli cells as an untagged, monomeric protein of 56 kDa. Its catalytic efficiency with oxalate, K (oxalate) M = 71.5 +/- 13.3 muM, V max = 8.2 +/- 0.8 mumole min(-1) mg(-1), was similar to that of OCS homologs from Arabidopsis thaliana (AtAAE3) and Medicago truncatula (MtAAE3). The enzyme was crystalized in complex with AMP and is the first OCS whose structure was determined in the thioester-forming conformation. Finally, we propose that substituting LsOCS with an oxalate oxidase or decarboxylase may reduce the levels of beta-ODAP in grass pea.

The identification and characterization of an oxalyl-CoA synthetase from grass pea (Lathyrus sativus L.).,Goldsmith M, Barad S, Peleg Y, Albeck S, Dym O, Brandis A, Mehlman T, Reich Z RSC Chem Biol. 2022 Feb 8;3(3):320-333. doi: 10.1039/d1cb00202c. eCollection 2022, Mar 9. PMID:35359497[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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References

  1. Goldsmith M, Barad S, Peleg Y, Albeck S, Dym O, Brandis A, Mehlman T, Reich Z. The identification and characterization of an oxalyl-CoA synthetase from grass pea (Lathyrus sativus L.). RSC Chem Biol. 2022 Feb 8;3(3):320-333. doi: 10.1039/d1cb00202c. eCollection 2022, Mar 9. PMID:35359497 doi:http://dx.doi.org/10.1039/d1cb00202c

Contents


PDB ID 6qjz

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