1i74

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1i74.gif|left|200px]]<br /><applet load="1i74" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1i74.gif|left|200px]]
-
caption="1i74, resolution 2.2&Aring;" />
+
 
-
'''STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE'''<br />
+
{{Structure
 +
|PDB= 1i74 |SIZE=350|CAPTION= <scene name='initialview01'>1i74</scene>, resolution 2.2&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</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]
 +
|GENE=
 +
}}
 +
 
 +
'''STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1I74 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I74 OCA].
+
1I74 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I74 OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11525166 11525166]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/11525166 11525166]
[[Category: Inorganic diphosphatase]]
[[Category: Inorganic diphosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 24: Line 33:
[[Category: hydrolase]]
[[Category: hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:38 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:46:21 2008''

Revision as of 09:46, 20 March 2008


PDB ID 1i74

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: , and
Activity: Inorganic diphosphatase, with EC number 3.6.1.1
Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 11:46:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools