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| - | [[Image:1qez.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1qez| PDB=1qez | SCENE= }} | | {{STRUCTURE_1qez| PDB=1qez | SCENE= }} |
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| - | '''SULFOLOBUS ACIDOCALDARIUS INORGANIC PYROPHOSPHATASE: AN ARCHAEL PYROPHOSPHATASE.'''
| + | ===SULFOLOBUS ACIDOCALDARIUS INORGANIC PYROPHOSPHATASE: AN ARCHAEL PYROPHOSPHATASE.=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10386872}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10386872 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10386872}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Magnesium]] | | [[Category: Magnesium]] |
| | [[Category: Thermostability]] | | [[Category: Thermostability]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:11:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:40:35 2008'' |
Revision as of 05:40, 28 July 2008
Template:STRUCTURE 1qez
SULFOLOBUS ACIDOCALDARIUS INORGANIC PYROPHOSPHATASE: AN ARCHAEL PYROPHOSPHATASE.
Template:ABSTRACT PUBMED 10386872
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
Page seeded by OCA on Mon Jul 28 08:40:35 2008
