1dy3
From Proteopedia
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| - | [[Image:1dy3.gif|left|200px]]<br /> | + | [[Image:1dy3.gif|left|200px]]<br /><applet load="1dy3" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1dy3" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1dy3, resolution 2.0Å" /> | caption="1dy3, resolution 2.0Å" /> | ||
'''TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.'''<br /> | '''TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.'''<br /> | ||
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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 MG, ATP and 87Y 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] | + | 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 MG, ATP and 87Y 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DY3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pyrophosphorylase]] | [[Category: pyrophosphorylase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:46:52 2007'' |
Revision as of 12:37, 18 December 2007
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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 with MG, ATP and 87Y as ligands. Active as 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, with EC number 2.7.6.3 Known structural/functional Sites: , , and . 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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