1dy3
From Proteopedia
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|PDB= 1dy3 |SIZE=350|CAPTION= <scene name='initialview01'>1dy3</scene>, resolution 2.0Å | |PDB= 1dy3 |SIZE=350|CAPTION= <scene name='initialview01'>1dy3</scene>, resolution 2.0Å | ||
|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> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5 | + | |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] | |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= | |GENE= | ||
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[[Category: pyrophosphorylase]] | [[Category: pyrophosphorylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:34:37 2008'' |
Revision as of 09:34, 23 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , and | ||||||
| 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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