1u1i

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[[Image:1u1i.jpg|left|200px]]<br /><applet load="1u1i" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1u1i.jpg|left|200px]]
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caption="1u1i, resolution 1.9&Aring;" />
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'''Myo-inositol phosphate synthase mIPS from A. fulgidus'''<br />
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{{Structure
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|PDB= 1u1i |SIZE=350|CAPTION= <scene name='initialview01'>1u1i</scene>, resolution 1.9&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Myo-inositol phosphate synthase mIPS from A. fulgidus'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1U1I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_dsm_4304 Archaeoglobus fulgidus dsm 4304] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U1I OCA].
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1U1I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_dsm_4304 Archaeoglobus fulgidus dsm 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U1I OCA].
==Reference==
==Reference==
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Reaching for mechanistic consensus across life kingdoms: structure and insights into catalysis of the myo-inositol-1-phosphate synthase (mIPS) from Archaeoglobus fulgidus., Stieglitz KA, Yang H, Roberts MF, Stec B, Biochemistry. 2005 Jan 11;44(1):213-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15628862 15628862]
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Reaching for mechanistic consensus across life kingdoms: structure and insights into catalysis of the myo-inositol-1-phosphate synthase (mIPS) from Archaeoglobus fulgidus., Stieglitz KA, Yang H, Roberts MF, Stec B, Biochemistry. 2005 Jan 11;44(1):213-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15628862 15628862]
[[Category: Archaeoglobus fulgidus dsm 4304]]
[[Category: Archaeoglobus fulgidus dsm 4304]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: NAD]]
[[Category: NAD]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: metal ions]]
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[[Category: metal ion]]
[[Category: nad cofactor]]
[[Category: nad cofactor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:26:05 2008''

Revision as of 12:26, 20 March 2008

Image:1u1i.jpg


PDB ID 1u1i

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



Myo-inositol phosphate synthase mIPS from A. fulgidus


Overview

myo-Inositol-1-phosphate synthase (mIPS) catalyzes the first step in the synthesis of l-myo-inositol-1-phosphate. We have solved and refined the structure of the mIPS from the hyperthermophilic sulfate reducer Archaeoglobus fulgidus at 1.9 A resolution. The enzyme crystallized from poly(ethylene glycol) in the P1 space group with one tetramer in the asymmetric unit and provided a view of the entire biologically active oligomer. Despite significant changes in sequence length and amino acid composition, the general architecture of the archaeal enzyme is similar to that of the eukaryotic mIPS from Saccharomyces cerevisiae and bacterial mIPS from Mycobacterium tuberculosis. The enhanced thermostability of the archaeal enzyme as compared to that from yeast is consistent with deletion of a number of surface loops that results in a significantly smaller protein. In the structure of the A. fulgidus mIPS, the active sites of all four subunits were fully ordered and contained NAD(+) and inorganic phosphate. The structure also contained a single metal ion (identified as K(+)) in two of the four subunits. The analysis of the electrostatic potential maps of the protein suggested the presence of a second metal-ion-binding site in close proximity to the first metal ion and NAD(+). The modeling of the substrate and known inhibitors suggests a critical role for the second metal ion in catalysis and provides insights into the common elements of the catalytic cycle in enzymes from different life kingdoms.

About this Structure

1U1I is a Single protein structure of sequence from Archaeoglobus fulgidus dsm 4304. Full crystallographic information is available from OCA.

Reference

Reaching for mechanistic consensus across life kingdoms: structure and insights into catalysis of the myo-inositol-1-phosphate synthase (mIPS) from Archaeoglobus fulgidus., Stieglitz KA, Yang H, Roberts MF, Stec B, Biochemistry. 2005 Jan 11;44(1):213-24. PMID:15628862

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