1YGZ

Crystal Structure of Inorganic Pyrophosphatase from Helicobacter pylori

Summary for 1YGZ

• Entry DOI: 10.2210/pdb1ygz/pdb
• Descriptor: Inorganic pyrophosphatase (2 entities in total)
• Functional Keywords: hydrolase
• Biological source: Helicobacter pylori
• Cellular location: Cytoplasm (By similarity): P56153
• Total number of polymer chains: 6
• Total formula weight: 116913.12

Authors

Wu, C.A.,Lokanath, N.K.,Kim, D.Y.,Park, H.J.,Hwang, H.Y.,Kim, S.T.,Suh, S.W.,Kim, K.K. (deposition date: 2005-01-06, release date: 2005-11-01, Last modification date: 2024-10-30)

Primary citation

Wu, C.A.,Lokanath, N.K.,Kim, D.Y.,Park, H.J.,Hwang, H.Y.,Kim, S.T.,Suh, S.W.,Kim, K.K.
Structure of inorganic pyrophosphatase from Helicobacter pylori.
Acta Crystallogr.,Sect.D, 61:1459-1464, 2005

PubMed Abstract: Inorganic pyrophosphatase (PPase) is a ubiquitous cytosolic enzyme which catalyzes the hydrolysis of inorganic pyrophosphate (PPi) to orthophosphate (Pi). The crystal structure of inorganic pyrophosphatase from Helicobacter pylori (H-PPase) has been solved by MAD and refined to an R factor of 20.6% at 2.6 A resolution. The crystallographic asymmetric unit contains a homohexameric H-PPase arranged as a dimer of trimers. While most of the structural elements of PPases are highly conserved in H-PPase, some unique structural features are localized in the flexible loops near the active site, suggesting that the structural flexibility of these loops is required for the catalytic efficiency of PPase.

PubMed: 16239722
DOI: 10.1107/S0907444905025667

Experimental method

X-RAY DIFFRACTION (2.6 Å)