| Literature DB >> 16239722 |
Chun Ai Wu1, Neratur K Lokanath, Dong Young Kim, Hye Jin Park, Hye Yeon Hwang, Seong Tae Kim, Se Won Suh, Kyeong Kyu Kim.
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.Entities:
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Year: 2005 PMID: 16239722 DOI: 10.1107/S0907444905025667
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449