1faj

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{{Structure
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|PDB= 1faj |SIZE=350|CAPTION= <scene name='initialview01'>1faj</scene>, resolution 2.15&Aring;
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The line below this paragraph, containing "STRUCTURE_1faj", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1faj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1faj OCA], [http://www.ebi.ac.uk/pdbsum/1faj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1faj RCSB]</span>
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'''INORGANIC PYROPHOSPHATASE'''
'''INORGANIC PYROPHOSPHATASE'''
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[[Category: Kankare, J A.]]
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[[Category: Salminen, T.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: inorganic pyrophosphatase]]
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[[Category: Inorganic pyrophosphatase]]
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[[Category: magnesium]]
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[[Category: Magnesium]]
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Revision as of 13:06, 2 May 2008

Image:1faj.gif


PDB ID 1faj

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1faj, resolution 2.15Å ()
Activity: Inorganic diphosphatase, with EC number 3.6.1.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



INORGANIC PYROPHOSPHATASE


Overview

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.

About this Structure

1FAJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 16:06:15 2008

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