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| - | [[Image:1i74.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1i74.png|left|200px]] |
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| | {{STRUCTURE_1i74| PDB=1i74 | SCENE= }} | | {{STRUCTURE_1i74| PDB=1i74 | SCENE= }} |
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| - | '''STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE'''
| + | ===STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE=== |
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| - | ==Overview==
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| - | BACKGROUND: Streptococcus mutans pyrophosphatase (Sm-PPase) is a member of a relatively uncommon but widely dispersed sequence family (family II) of inorganic pyrophosphatases. A structure will answer two main questions: is it structurally similar to the family I PPases, and is the mechanism similar? RESULTS: The first family II PPase structure, that of homodimeric Sm-PPase complexed with metal and sulfate ions, has been solved by X-ray crystallography at 2.2 A resolution. The tertiary fold of Sm-PPase consists of a 189 residue alpha/beta N-terminal domain and a 114 residue mixed beta sheet C-terminal domain and bears no resemblance to family I PPase, even though the arrangement of active site ligands and the residues that bind them shows significant similarity. The preference for Mn2+ over Mg2+ in family II PPases is explained by the histidine ligands and bidentate carboxylate coordination. The active site is located at the domain interface. The C-terminal domain is hinged to the N-terminal domain and exists in both closed and open conformations. CONCLUSIONS: The active site similiarities, including a water coordinated to two metal ions, suggest that the family II PPase mechanism is "analogous" (not "homologous") to that of family I PPases. This is a remarkable example of convergent evolution. The large change in C-terminal conformation suggests that domain closure might be the mechanism by which Sm-PPase achieves specificity for pyrophosphate over other polyphosphates.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11525166}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11525166 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11525166}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Salminen, A.]] | | [[Category: Salminen, A.]] |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:39:07 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:30:54 2008'' |
Revision as of 07:30, 1 July 2008
Template:STRUCTURE 1i74
STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE
Template:ABSTRACT PUBMED 11525166
About this Structure
1I74 is a Single protein structure of sequence from Streptococcus mutans. Full crystallographic information is available from OCA.
Reference
Crystal structure of Streptococcus mutans pyrophosphatase: a new fold for an old mechanism., Merckel MC, Fabrichniy IP, Salminen A, Kalkkinen N, Baykov AA, Lahti R, Goldman A, Structure. 2001 Apr 4;9(4):289-97. PMID:11525166
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