1rao: Difference between revisions

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[[Image:1rao.gif|left|200px]]<br /><applet load="1rao" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1rao.gif|left|200px]]
caption="1rao, resolution 1.56&Aring;" />
 
'''CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI HPPK WITH AMP AND 6-HYDROXYMETHYLPTERIN-DIPHOSPHATE AT 1.56 ANGSTROM RESOLUTION'''<br />
{{Structure
|PDB= 1rao |SIZE=350|CAPTION= <scene name='initialview01'>1rao</scene>, resolution 1.56&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=HH2:6-HYDROXYMETHYLPTERIN-DIPHOSPHATE'>HH2</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine_diphosphokinase 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.3 2.7.6.3]
|GENE= FOLK, B0142 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI HPPK WITH AMP AND 6-HYDROXYMETHYLPTERIN-DIPHOSPHATE AT 1.56 ANGSTROM RESOLUTION'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1RAO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=HH2:'>HH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine_diphosphokinase 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.3 2.7.6.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RAO OCA].  
1RAO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RAO OCA].  


==Reference==
==Reference==
Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase., Blaszczyk J, Shi G, Li Y, Yan H, Ji X, Structure. 2004 Mar;12(3):467-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15016362 15016362]
Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase., Blaszczyk J, Shi G, Li Y, Yan H, Ji X, Structure. 2004 Mar;12(3):467-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15016362 15016362]
[[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]]
[[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
Line 34: Line 43:
[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]


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Revision as of 14:49, 20 March 2008

File:1rao.gif


PDB ID 1rao

Drag the structure with the mouse to rotate
, resolution 1.56Å
Ligands: and
Gene: FOLK, B0142 (Escherichia coli)
Activity: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, with EC number 2.7.6.3
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI HPPK WITH AMP AND 6-HYDROXYMETHYLPTERIN-DIPHOSPHATE AT 1.56 ANGSTROM RESOLUTION


OverviewOverview

6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the Mg(2+)-dependent pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). The reaction follows a bi-bi mechanism with ATP as the first substrate and AMP and HP pyrophosphate (HPPP) as the two products. HPPK is a key enzyme in the folate biosynthetic pathway and is essential for microorganisms but absent from mammals. For the HPPK-catalyzed pyrophosphoryl transfer, a reaction coordinate is constructed on the basis of the thermodynamic and transient kinetic data we reported previously, and the reaction trajectory is mapped out with five three-dimensional structures of the enzyme at various liganded states. The five structures are apo-HPPK (ligand-free enzyme), HPPK.MgATP(analog) (binary complex of HPPK with its first substrate) and HPPK.MgATP(analog).HP (ternary complex of HPPK with both substrates), which we reported previously, and HPPK.AMP.HPPP (ternary complex of HPPK with both product molecules) and HPPK.HPPP (binary complex of HPPK with one product), which we present in this study.

About this StructureAbout this Structure

1RAO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase., Blaszczyk J, Shi G, Li Y, Yan H, Ji X, Structure. 2004 Mar;12(3):467-75. PMID:15016362

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