1dy3

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|PDB= 1dy3 |SIZE=350|CAPTION= <scene name='initialview01'>1dy3</scene>, resolution 2.0&Aring;
|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>
|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>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=87Y:7,8-DIHYDRO-6-HYDROXYMETHYL-7-METHYL-7-[2-PHENYLETHYL]-PTERIN'>87Y</scene>
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|LIGAND= <scene name='pdbligand=87Y:7,8-DIHYDRO-6-HYDROXYMETHYL-7-METHYL-7-[2-PHENYLETHYL]-PTERIN'>87Y</scene>, <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dy3 OCA], [http://www.ebi.ac.uk/pdbsum/1dy3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dy3 RCSB]</span>
}}
}}
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[[Category: Somers, D O.]]
[[Category: Somers, D O.]]
[[Category: Stammers, D K.]]
[[Category: Stammers, D K.]]
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[[Category: 87Y]]
 
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[[Category: ATP]]
 
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[[Category: MG]]
 
[[Category: de novo folate biosynthesis]]
[[Category: de novo folate biosynthesis]]
[[Category: pyrophosphorylase]]
[[Category: pyrophosphorylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:34:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:51:05 2008''

Revision as of 16:51, 30 March 2008


PDB ID 1dy3

Drag the structure with the mouse to rotate
, resolution 2.0Å
Sites: , , and
Ligands: , ,
Activity: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, with EC number 2.7.6.3
Resources: FirstGlance, OCA, PDBsum, RCSB
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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