2CMH

Crystal Structure of Spermidine Synthase from Helicobacter Pylori

Summary for 2CMH

• Entry DOI: 10.2210/pdb2cmh/pdb
• Related: 2CMG
• Descriptor: SPERMIDINE SYNTHASE (2 entities in total)
• Functional Keywords: putrescine aminopropyltransferase, spermidine biosynthesis, spee, transferase, spermidine synthase, helicobacter pylori, polyamine biosynthesis
• Biological source: HELICOBACTER PYLORI
• Total number of polymer chains: 3
• Total formula weight: 91756.85

Authors

Sun, Y.-J.,Lu, P.-K. (deposition date: 2006-05-08, release date: 2007-05-08, Last modification date: 2024-05-08)

Primary citation

Lu, P.-K.,Tsai, J.-Y.,Chien, H.Y.,Huang, H.,Chu, C.-H.,Sun, Y.-J.
Crystal Structure of Helicobacter Pylori Spermidine Synthase: A Rossmann-Like Fold with a Distinct Active Site
Proteins: Struct., Funct., Bioinf., 67:743-, 2007

PubMed Abstract: Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the transfer of the aminopropyl group from decarboxylated S-adenosylmethionine to putrescine during spermidine biosynthesis. Helicobacter pylori PAPT (HpPAPT) has a low sequence identity with other PAPTs and lacks the signature sequence found in other PAPTs. The crystal structure of HpPAPT, determined by multiwavelength anomalous dispersion, revealed an N-terminal beta-stranded domain and a C-terminal Rossmann-like domain. Structural comparison with other PAPTs showed that HpPAPT has a unique binding pocket between two domains, numerous non-conserved residues, a less acidic electrostatic surface potential, and a large buried space within the structure. HpPAPT lacks the gatekeeping loop that facilitates substrate binding in other PAPTs. PAPTs are essential for bacterial cell viability; thus, HpPAPT may be a potential antimicrobial drug target for H. pylori owing to its characteristic PAPT sequence and distinct conformation.

PubMed: 17357156
DOI: 10.1002/PROT.21315

Experimental method

X-RAY DIFFRACTION (2.3 Å)