1nv3: Difference between revisions

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[[Image:1nv3.gif|left|200px]]<br /><applet load="1nv3" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1nv3.gif|left|200px]]
caption="1nv3, resolution 2.0&Aring;" />
 
'''Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate and Thallium (100 mM)'''<br />
{{Structure
|PDB= 1nv3 |SIZE=350|CAPTION= <scene name='initialview01'>1nv3</scene>, resolution 2.0&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=TL:THALLIUM (I) ION'>TL</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11]
|GENE=
}}
 
'''Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate and Thallium (100 mM)'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1NV3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=F6P:'>F6P</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=TL:'>TL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NV3 OCA].  
1NV3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NV3 OCA].  


==Reference==
==Reference==
Interaction of Tl+ with product complexes of fructose-1,6-bisphosphatase., Choe JY, Nelson SW, Fromm HJ, Honzatko RB, J Biol Chem. 2003 May 2;278(18):16008-14. Epub 2003 Feb 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595529 12595529]
Interaction of Tl+ with product complexes of fructose-1,6-bisphosphatase., Choe JY, Nelson SW, Fromm HJ, Honzatko RB, J Biol Chem. 2003 May 2;278(18):16008-14. Epub 2003 Feb 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595529 12595529]
[[Category: Fructose-bisphosphatase]]
[[Category: Fructose-bisphosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: PO4]]
[[Category: PO4]]
[[Category: TL]]
[[Category: TL]]
[[Category: allosteric enzymes]]
[[Category: allosteric enzyme]]
[[Category: bisphosphatase]]
[[Category: bisphosphatase]]
[[Category: gluconeogenesis]]
[[Category: gluconeogenesis]]
[[Category: hydrolase]]
[[Category: hydrolase]]


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Revision as of 14:02, 20 March 2008

File:1nv3.gif


PDB ID 1nv3

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: , , and
Activity: Fructose-bisphosphatase, with EC number 3.1.3.11
Coordinates: save as pdb, mmCIF, xml



Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate and Thallium (100 mM)


OverviewOverview

Fructose-1,6-bisphosphatase requires divalent cations (Mg2+, Mn2+, or Zn2+) for catalysis, but a diverse set of monovalent cations (K+, Tl+, Rb+, or NH(4)(+)) will further enhance enzyme activity. Here, the interaction of Tl+ with fructose-1,6-bisphosphatase is explored under conditions that support catalysis. On the basis of initial velocity kinetics, Tl+ enhances catalysis by 20% with a K(a) of 1.3 mm and a Hill coefficient near unity. Crystal structures of enzyme complexes with Mg2+, Tl+, and reaction products, in which the concentration of Tl+ is 1 mm or less, reveal Mg2+ at metal sites 1, 2, and 3 of the active site, but little or no bound Tl+. Intermediate concentrations of Tl+ (5-20 mm) displace Mg2+ from site 3 and the 1-OH group of fructose 6-phosphate from in-line geometry with respect to bound orthophosphate. Loop 52-72 appears in a new conformational state, differing from its engaged conformation by disorder in residues 61-69. Tl+ does not bind to metal sites 1 or 2 in the presence of Mg2+, but does bind to four other sites with partial occupancy. Two of four Tl+ sites probably represent alternative binding sites for the site 3 catalytic Mg2+, whereas the other sites could play roles in monovalent cation activation.

About this StructureAbout this Structure

1NV3 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

Interaction of Tl+ with product complexes of fructose-1,6-bisphosphatase., Choe JY, Nelson SW, Fromm HJ, Honzatko RB, J Biol Chem. 2003 May 2;278(18):16008-14. Epub 2003 Feb 20. PMID:12595529

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