1i74

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[[Image:1i74.gif|left|200px]]
[[Image:1i74.gif|left|200px]]
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{{Structure
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|PDB= 1i74 |SIZE=350|CAPTION= <scene name='initialview01'>1i74</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1i74", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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{{STRUCTURE_1i74| PDB=1i74 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i74 OCA], [http://www.ebi.ac.uk/pdbsum/1i74 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i74 RCSB]</span>
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'''STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE'''
'''STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE'''
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[[Category: Merckel, M C.]]
[[Category: Merckel, M C.]]
[[Category: Salminen, A.]]
[[Category: Salminen, A.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:39:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:15:31 2008''
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Revision as of 16:39, 2 May 2008

Image:1i74.gif

Template:STRUCTURE 1i74

STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE


Overview

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.

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 Page seeded by OCA on Fri May 2 19:39:07 2008

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