1qez
From Proteopedia
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|PDB= 1qez |SIZE=350|CAPTION= <scene name='initialview01'>1qez</scene>, resolution 2.70Å | |PDB= 1qez |SIZE=350|CAPTION= <scene name='initialview01'>1qez</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qez OCA], [http://www.ebi.ac.uk/pdbsum/1qez PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qez RCSB]</span> | ||
}} | }} | ||
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[[Category: Nummelin, H.]] | [[Category: Nummelin, H.]] | ||
[[Category: Schafer, G.]] | [[Category: Schafer, G.]] | ||
| - | [[Category: MG]] | ||
[[Category: inorganic pyrophosphatase]] | [[Category: inorganic pyrophosphatase]] | ||
[[Category: magnesium]] | [[Category: magnesium]] | ||
[[Category: thermostability]] | [[Category: thermostability]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:30 2008'' |
Revision as of 20:12, 30 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Inorganic diphosphatase, with EC number 3.6.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SULFOLOBUS ACIDOCALDARIUS INORGANIC PYROPHOSPHATASE: AN ARCHAEL PYROPHOSPHATASE.
Overview
The first crystal structure of an inorganic pyrophosphatase (S-PPase) from an archaebacterium, the thermophile Sulfolobus acidocaldarius, has been solved by molecular replacement and refined to an R-factor of 19.7% at 2.7 A. S-PPase is a D3 homohexameric protein with one Mg2+ per active site in a position similar to, but not identical with, the first activating metal in mesophilic pyrophosphatases (PPase). In mesophilic PPases, Asp65, Asp70, and Asp102 coordinate the Mg2+, while only Asp65 and Asp102 do in S-PPase, and the Mg2+ moves by 0.7 A. S-PPase may therefore be deactivated at low temperature by mispositioning a key metal ion. The monomer S-PPase structure is very similar to that of Thermus thermophilus (T-PPase) and Escherichia coli (E-PPase), root-mean-square deviations around 1 A/Calpha. But the hexamer structures of S- and T-PPase are more tightly packed and more similar to each other than they are to that of E-PPase, as shown by the increase in surface area buried upon oligomerization. In T-PPase, Arg116 creates an interlocking ionic network to both twofold and threefold related monomers; S-PPase has hydrophilic interactions to threefold related monomers absent in both E- and T-PPase. In addition, the thermostable PPases have about 7% more hydrogen bonds per monomer than E-PPase, and, especially in S-PPase, additional ionic interactions anchor the C-terminus to the rest of the protein. Thermostability in PPases is thus due to subtle improvements in both monomer and oligomer interactions.
About this Structure
1QEZ is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.
Reference
Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase., Leppanen VM, Nummelin H, Hansen T, Lahti R, Schafer G, Goldman A, Protein Sci. 1999 Jun;8(6):1218-31. PMID:10386872
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