1P3C

Glutamyl endopeptidase from Bacillus intermedius

Summary for 1P3C

• Entry DOI: 10.2210/pdb1p3c/pdb
• Related: 1P3E
• Descriptor: glutamyl-endopeptidase (2 entities in total)
• Functional Keywords: serine protease, hydrolase
• Biological source: Bacillus intermedius
• Total number of polymer chains: 1
• Total formula weight: 22783.11

Authors

Meijers, R.,Blagova, E.V.,Levdikov, V.M.,Rudenskaya, G.N.,Chestukhina, G.G.,Akimkina, T.V.,Kostrov, S.V.,Lamzin, V.S.,Kuranova, I.P. (deposition date: 2003-04-17, release date: 2004-04-27, Last modification date: 2024-11-13)

Primary citation

Meijers, R.,Blagova, E.V.,Levdikov, V.M.,Rudenskaya, G.N.,Chestukhina, G.G.,Akimkina, T.V.,Kostrov, S.V.,Lamzin, V.S.,Kuranova, I.P.
The crystal structure of glutamyl endopeptidase from Bacillus intermedius reveals a structural link between zymogen activation and charge compensation.
Biochemistry, 43:2784-2791, 2004

PubMed Abstract: Extracellular glutamyl endopeptidase from Bacillus intermedius (BIEP) is a chymotrypsin-like serine protease which cleaves the peptide bond on the carboxyl side of glutamic acid. Its three-dimensional structure was determined for C222(1) and C2 crystal forms of BIEP to 1.5 and 1.75 A resolution, respectively. The topology of BIEP diverges from the most common chymotrypsin architecture, because one of the domains consists of a beta-sandwich consisting of two antiparallel beta-sheets and two helices. In the C2 crystals, a 2-methyl-2,4-pentanediol (MPD) molecule was found in the substrate binding site, mimicking a glutamic acid. This enabled the identification of the residues involved in the substrate recognition. The presence of the MPD molecule causes a change in the active site; the interaction between two catalytic residues (His47 and Ser171) is disrupted. The N-terminal end of the enzyme is involved in the formation of the substrate binding pocket. This indicates a direct relation between zymogen activation and substrate charge compensation.

PubMed: 15005613
DOI: 10.1021/bi035354s

Experimental method

X-RAY DIFFRACTION (1.5 Å)