1dy3

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[[Image:1dy3.gif|left|200px]]
 
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{{Structure
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==Ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue.==
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|PDB= 1dy3 |SIZE=350|CAPTION= <scene name='initialview01'>1dy3</scene>, resolution 2.0&Aring;
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<StructureSection load='1dy3' size='340' side='right'caption='[[1dy3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|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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== Structural highlights ==
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|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>
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<table><tr><td colspan='2'>[[1dy3]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DY3 FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=87Y:7,8-DIHYDRO-6-HYDROXYMETHYL-7-METHYL-7-[2-PHENYLETHYL]-PTERIN'>87Y</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dy3 OCA], [https://pdbe.org/1dy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dy3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dy3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HPPK_ECOLI HPPK_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/1dy3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dy3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.'''
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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<ref>PMID:10452528</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1dy3" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[HPPK 3D structures|HPPK 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Achari, A.]]
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[[Category: Achari A]]
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[[Category: Bryant, P K.]]
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[[Category: Bryant PK]]
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[[Category: Champness, J N.]]
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[[Category: Champness JN]]
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[[Category: Rosemond, J.]]
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[[Category: Rosemond J]]
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[[Category: Scott, D L.]]
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[[Category: Scott DL]]
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[[Category: Somers, D O.]]
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[[Category: Somers DO]]
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[[Category: Stammers, D K.]]
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[[Category: Stammers DK]]
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[[Category: 87Y]]
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[[Category: ATP]]
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[[Category: MG]]
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[[Category: de novo folate biosynthesis]]
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[[Category: pyrophosphorylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:46:19 2008''
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Current revision

Ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue.

PDB ID 1dy3

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