PDBsum entry 3vz3

Oxidoreductase

PDB id: 3vz3

Contents

Protein chains

453 a.a.

Ligands

SSN ×2

NAP ×2

Waters ×1149

PDB id:

3vz3

Name:

Oxidoreductase

Title:

Structural insights into substrate and cofactor selection by sp2771

Structure:

Succinate-semialdehyde dehydrogenase. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Synechococcus. Organism_taxid: 32049. Strain: atcc 27264 / pcc 7002 / pr-6. Gene: synpcc7002_a2771. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.69Å R-factor: 0.168 R-free: 0.203

Authors:

Y.A.Yuan,Z.Yuan,B.Yin,D.Wei

Key ref:

Z.Yuan et al. (2013). Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase. J Struct Biol, 182, 125-135. PubMed id: 23500184 DOI: 10.1016/j.jsb.2013.03.001

Date:

09-Oct-12 Release date: 10-Jul-13

Protein chains

B1XMM6  (B1XMM6_SYNP2) -  Succinate-semialdehyde dehydrogenase from Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)

Seq: 454 a.a.

Struc: 453 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/j.jsb.2013.03.001

J Struct Biol 182:125-135 (2013)

PubMed id: 23500184

Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase.

Z.Yuan, B.Yin, D.Wei, Y.R.Yuan.

ABSTRACT

Aldehyde dehydrogenase (ALDH) catalyzes the oxidation of aldehydes to carboxylic acids. Cyanobacterium Synechococcus contains one ALDH enzyme (Sp2771), together with a novel 2-oxoglutarate decarboxylase, to complete a non-canonical tricarboxylic acid cycle. However, the molecular mechanisms for substrate selection and cofactor preference by Sp2771 are largely unknown. Here, we report crystal structures of wild type Sp2771, Sp2771 S419A mutant and ternary structure of Sp2771 C262A mutant in complex with NADP(+) and SSA, as well as binary structure of Gluconobacter oxydans aldehyde dehydrogenase (Gox0499) in complex with PEG. Structural comparison of Sp2771 with Gox0499, coupled with mutational analysis, demonstrates that Ser157 residue in Sp2771 and corresponding Pro159 residue in Gox0499 play critical structural roles in determining NADP(+) and NAD(+) preference for Sp2771 and Gox0499, respectively, whereas size and distribution of hydrophobic residues along the substrate binding funnel determine substrate selection. Hence, our work has provided insightful structural information into cofactor and substrate selection by ALDH.