1LF6

CRYSTAL STRUCTURE OF BACTERIAL GLUCOAMYLASE

Summary for 1LF6

• Entry DOI: 10.2210/pdb1lf6/pdb
• Related: 1AYX 1LF9 3GLY
• Descriptor: glucoamylase, SULFATE ION (3 entities in total)
• Functional Keywords: (alpha/alpha) barrel, 6 alpha-helical hairpin torroid, super beta sandwich, carbohydrase family gh15, hydrolase
• Biological source: Thermoanaerobacterium thermosaccharolyticum
• Total number of polymer chains: 2
• Total formula weight: 153373.13

Authors

Aleshin, A.E.,Feng, P.-H.,Honzatko, R.B.,Reilly, P.J. (deposition date: 2002-04-10, release date: 2003-02-25, Last modification date: 2024-02-14)

Primary citation

Aleshin, A.E.,Feng, P.-H.,Honzatko, R.B.,Reilly, P.J.
Crystal structure and evolution of prokaryotic glucoamylase
J.Mol.Biol., 327:61-73, 2003

PubMed Abstract: The first crystal structures of a two-domain, prokaryotic glucoamylase were determined to high resolution from the clostridial species Thermoanaerobacterium thermosaccharolyticum with and without acarbose. The N-terminal domain has 18 antiparallel strands arranged in beta-sheets of a super-beta-sandwich. The C-terminal domain is an (alpha/alpha)(6) barrel, lacking the peripheral subdomain of eukaryotic glucoamylases. Interdomain contacts are common to all prokaryotic Family GH15 proteins. Domains similar to those of prokaryotic glucoamylases in maltose phosphorylases (Family GH65) and glycoaminoglycan lyases (Family PL8) suggest evolution from a common ancestor. Eukaryotic glucoamylases may have evolved from prokaryotic glucoamylases by the substitution of the N-terminal domain with the peripheral subdomain and by the addition of a starch-binding domain.

PubMed: 12614608
DOI: 10.1016/S0022-2836(03)00084-6

Experimental method

X-RAY DIFFRACTION (2.1 Å)