2eip | pdb_00002eip

INORGANIC PYROPHOSPHATASE

spinqualitylabelsall models 2eip, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2eip is a 2 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1eip. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Inorganic diphosphatase, with EC number 3.6.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The refined crystal structures of hexameric soluble inorganic pyrophosphatase from E. coli (E-PPase) are reported to R factors of 18.7 and 18.3% at 2.15 and 2.2 A, respectively. The first contains one independent monomer; the other, two independent monomers, in an R32 unit cell. Because the E-PPase monomer is small with a large open active site, there are relatively few hydrophobic interactions that connect the active-site loops to the five-stranded twisted beta-barrel that is the hydrophobic core of the molecule. The active-site loops are, however, held in place by interactions between monomers around the threefold and twofold symmetry axes of the D(3) hexamer. Consequently, mutations of active-site residues (such as Glu20 and Lysl04) often affect protein stability and oligomeric structure. Conversely, mutations of residues in the interface between monomers (such as His136 and Hisl40) not only affect oligomeric structure but also affect active-site function. The effects of the H136Q and H140Q variants can be explained by the extended ionic interaction between H140, D143 and H136' of the neighbouring monomer. This interaction is further buttressed by an extensive hydrogen-bonding network that appears to explain why the E-PPase hexamer is so stable and also why the H136Q and H140Q variant proteins are less stable as hexamers. Structure of Escherichia coli inorganic pyrophosphatase at 2.2 A resolution.,Kankare J, Salminen T, Lahti R, Cooperman BS, Baykov AA, Goldman A Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):551-63. PMID:15299678 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Inorganic pyrophosphatase 3D structures

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