1dy3: Difference between revisions

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[[Image:1dy3.gif|left|200px]]<br /><applet load="1dy3" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1dy3.gif|left|200px]]
caption="1dy3, resolution 2.0&Aring;" />
 
'''TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.'''<br />
{{Structure
|PDB= 1dy3 |SIZE=350|CAPTION= <scene name='initialview01'>1dy3</scene>, resolution 2.0&Aring;
|SITE= <scene name='pdbsite=AC1:Atp+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>AC1</scene>, <scene name='pdbsite=AC2:87y+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+Co+...'>AC3</scene> and <scene name='pdbsite=AC4:Mg+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+Co+...'>AC4</scene>
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=87Y:7,8-DIHYDRO-6-HYDROXYMETHYL-7-METHYL-7-[2-PHENYLETHYL]-PTERIN'>87Y</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=
}}
 
'''TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1DY3 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=MG:'>MG</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=87Y:'>87Y</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] Known structural/functional Sites: <scene name='pdbsite=AC1:Atp+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>AC1</scene>, <scene name='pdbsite=AC2:87y+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+Co+...'>AC3</scene> and <scene name='pdbsite=AC4:Mg+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+Co+...'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DY3 OCA].  
1DY3 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=1DY3 OCA].  


==Reference==
==Reference==
2.0 A X-ray structure of the ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue., Stammers DK, Achari A, Somers DO, Bryant PK, Rosemond J, Scott DL, Champness JN, FEBS Lett. 1999 Jul 30;456(1):49-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10452528 10452528]
2.0 A X-ray structure of the ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue., Stammers DK, Achari A, Somers DO, Bryant PK, Rosemond J, Scott DL, Champness JN, FEBS Lett. 1999 Jul 30;456(1):49-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10452528 10452528]
[[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]]
[[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: pyrophosphorylase]]
[[Category: pyrophosphorylase]]


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Revision as of 08:46, 20 March 2008

File:1dy3.gif


Drag the structure with the mouse to rotate
1dy3, resolution 2.0Å
Sites: AC1, AC2, AC3 and AC4
Ligands: MG, ATP and 87Y
Activity: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, with EC number 2.7.6.3
Coordinates: save as pdb, mmCIF, xml



TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.


Overview

The X-ray crystal structure of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase (PPPK) in a ternary complex with ATP and a pterin analogue has been solved to 2.0 A resolution, giving, for the first time, detailed information of the PPPK/ATP intermolecular interactions and the accompanying conformational change. The first 100 residues of the 158 residue peptide contain a betaalpha betabeta alphabeta motif present in several other proteins including nucleoside diphosphate kinase. Comparative sequence examination of a wide range of prokaryotic and lower eukaryotic species confirms the conservation of the PPPK active site, indicating the value of this de novo folate biosynthesis pathway enzyme as a potential target for the development of novel broad-spectrum anti-infective agents.

About this Structure

1DY3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

2.0 A X-ray structure of the ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue., Stammers DK, Achari A, Somers DO, Bryant PK, Rosemond J, Scott DL, Champness JN, FEBS Lett. 1999 Jul 30;456(1):49-53. PMID:10452528

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