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PDBsum entry 1eip

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Acid anhydride hydrolase PDB id
1eip
Contents
Protein chains
169 a.a.

References listed in PDB file
Key reference
Title The structure of e.Coli soluble inorganic pyrophosphatase at 2.7 a resolution.
Authors J.Kankare, G.S.Neal, T.Salminen, T.Glumoff, T.].Glumhoff t [corrected to glumoff, B.S.Cooperman, R.Lahti, A.Goldman.
Ref. Protein Eng, 1994, 7, 823-830.
PubMed id 7971944
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 70%.
Abstract
The structure of E.coli soluble inorganic pyrophosphatase has been refined at 2.7 A resolution to an R-factor of 20.9%. The overall fold of the molecule is essentially the same as yeast pyrophosphatase, except that yeast pyrophosphatase is longer at both the N- and C-termini. Escherichia coli pyrophosphatase is a mixed alpha + beta protein with a complicated topology. The active site cavity, which is also very similar to the yeast enzyme, is formed by seven beta-strands and an alpha-helix and has a rather asymmetric distribution of charged residues. Our structure-based alignment extends and improves upon earlier sequence alignment studies; it shows that probably no more than 14, not 15-17 charged and polar residues are part of the conserved enzyme mechanism of pyrophosphatases. Six of these conserved residues, at the bottom of the active site cavity, form a tight group centred on Asp70 and probably bind the two essential Mg2+ ions. The others, more spreadout and more positively charged, presumably bind substrate. Escherichia coli pyrophosphatase has an extra aspartate residue in the active site cavity, which may explain why the two enzymes bind divalent cation differently. Based on the structure, we have identified a sequence motif that seems to occur only in soluble inorganic pyrophosphatases.
Secondary reference #1
Title Evolutionary conservation of the active site of soluble inorganic pyrophosphatase.
Authors B.S.Cooperman, A.A.Baykov, R.Lahti.
Ref. Trends Biochem Sci, 1992, 17, 262-266.
PubMed id 1323891
Abstract
Secondary reference #2
Title Cloning and characterization of the gene encoding inorganic pyrophosphatase of escherichia coli k-12.
Authors R.Lahti, T.Pitkäranta, E.Valve, I.Ilta, E.Kukko-Kalske, J.Heinonen.
Ref. J Bacteriol, 1988, 170, 5901-5907.
PubMed id 2848015
Abstract
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