1dy3: Difference between revisions

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[[Image:1dy3.gif|left|200px]]
[[Image:1dy3.gif|left|200px]]


{{Structure
<!--
|PDB= 1dy3 |SIZE=350|CAPTION= <scene name='initialview01'>1dy3</scene>, resolution 2.0&Aring;
The line below this paragraph, containing "STRUCTURE_1dy3", creates the "Structure Box" on the page.
|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>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|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>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1dy3| PDB=1dy3  | SCENE= }}  
|RELATEDENTRY=
|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>
}}


'''TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.'''
'''TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.'''
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[[Category: Somers, D O.]]
[[Category: Somers, D O.]]
[[Category: Stammers, D K.]]
[[Category: Stammers, D K.]]
[[Category: de novo folate biosynthesis]]
[[Category: De novo folate biosynthesis]]
[[Category: pyrophosphorylase]]
[[Category: Pyrophosphorylase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:25:18 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:51:05 2008''

Revision as of 11:25, 2 May 2008

File:1dy3.gif

Template:STRUCTURE 1dy3

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 Page seeded by OCA on Fri May 2 14:25:18 2008

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