3BS8

Crystal structure of Glutamate 1-Semialdehyde Aminotransferase complexed with pyridoxamine-5'-phosphate From Bacillus subtilis

Summary for 3BS8

• Entry DOI: 10.2210/pdb3bs8/pdb
• Descriptor: Glutamate-1-semialdehyde 2,1-aminomutase, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: glutamate-1-semialdehyde 2, 1-aminotransferase, porphyrin biosynthesis, isomerase, pyridoxal phosphate
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (Potential): P30949
• Total number of polymer chains: 1
• Total formula weight: 47772.98

Authors

Ge, H.,Fan, J.,Teng, M.,Niu, L. (deposition date: 2007-12-22, release date: 2008-12-23, Last modification date: 2023-11-01)

Primary citation

Ge, H.,Lv, X.,Fan, J.,Gao, Y.,Teng, M.,Niu, L.
Crystal structure of Glutamate1-semialdehyde aminotransferase from Bacillus subtilis with bound pyridoxamine-5'-phosphate
Biochem.Biophys.Res.Commun., 402:356-360, 2010

PubMed Abstract: Glutamate-1-semialdehyde aminotransferase (GSA-AT), also named glutamate-1-semialdehyde aminomutase (GSAM), a pyridoxamine-5'-phosphate (PMP)/pyridoxal-5'-phosphate (PLP) dependent enzyme, catalyses the transamination of the substrate glutamate-1-semialdehyde (GSA) to the product 5-Aminolevulinic acid (ALA) by an unusual intramolecular exchange of amino and oxo groups within the catalytic intermediate 4,5-diaminovalerate (DAVA). This paper presents the crystal structure of GSA-AT from Bacillus subtilis (GSA-ATBsu) in its PMP-bound form at 2.3Å resolution. The structure was determined by molecular replacement using the Synechococcus GSAM (GSAMSyn) structure as a search model. Unlike the previous reported GSAM/GSA-AT structures, GSA-ATBsu is a symmetric homodimer in the PMP-bound form, which shows the structural symmetry at the gating loop region with open state, as well as identical cofactor (PMP) binding in each monomer. This observation of PMP in combination with an "open" lid supports one characteristic feature for this enzyme, as the catalyzed reaction is believed to be initiated by PMP. Furthermore, the symmetry of GSA-ATBsu structure challenges the previously proposed negative cooperativity between monomers of this enzyme.

PubMed: 20946885
DOI: 10.1016/j.bbrc.2010.10.033

Experimental method

X-RAY DIFFRACTION (2.3 Å)