6OUX

Structure of SMUL_1544, a decarboxylase from Sulfurospirillum multivorans

Summary for 6OUX

• Entry DOI: 10.2210/pdb6oux/pdb
• Descriptor: Threonine phosphate decarboxylase-like enzyme (2 entities in total)
• Functional Keywords: decarboxylase, smul_1544, ethanolamine o-phosphate, lyase
• Biological source: Sulfurospirillum multivorans
• Total number of polymer chains: 2
• Total formula weight: 90244.32

Authors

Wetterhorn, K.M.,Rayment, I.,Vecellio, A.,Seeger, M.,Keller, S.,Schubert, T. (deposition date: 2019-05-05, release date: 2019-06-05, Last modification date: 2023-10-11)

Primary citation

Keller, S.,Wetterhorn, K.M.,Vecellio, A.,Seeger, M.,Rayment, I.,Schubert, T.
Structural and functional analysis of an l-serine O-phosphate decarboxylase involved in norcobamide biosynthesis.
Febs Lett., 593:3040-3053, 2019

PubMed Abstract: Structural diversity of natural cobamides (Cbas, B vitamers) is limited to the nucleotide loop. The loop is connected to the cobalt-containing corrin ring via an (R)-1-aminopropan-2-ol O-2-phosphate (AP-P) linker moiety. AP-P is produced by the l-threonine O-3-phosphate (l-Thr-P) decarboxylase CobD. Here, the CobD homolog SMUL_1544 of the organohalide-respiring epsilonproteobacterium Sulfurospirillum multivorans was characterized as a decarboxylase that produces ethanolamine O-phosphate (EA-P) from l-serine O-phosphate (l-Ser-P). EA-P is assumed to serve as precursor of the linker moiety of norcobamides that function as cofactors in the respiratory reductive dehalogenase. SMUL_1544 (SmCobD) is a pyridoxal-5'-phosphate (PLP)-containing enzyme. The structural analysis of the SmCobD apoprotein combined with the characterization of truncated mutant proteins uncovered a role of the SmCobD N-terminus in efficient l-Ser-P conversion.

PubMed: 31325159
DOI: 10.1002/1873-3468.13543

Experimental method

X-RAY DIFFRACTION (1.94 Å)