1hka

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[[Image:1hka.jpg|left|200px]]
 
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==6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE==
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The line below this paragraph, containing "STRUCTURE_1hka", creates the "Structure Box" on the page.
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<StructureSection load='1hka' size='340' side='right'caption='[[1hka]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1hka]] 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=1HKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HKA FirstGlance]. <br>
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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]] 1.5&#8491;</td></tr>
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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=1hka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hka OCA], [https://pdbe.org/1hka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hka RCSB], [https://www.ebi.ac.uk/pdbsum/1hka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hka ProSAT]</span></td></tr>
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{{STRUCTURE_1hka| PDB=1hka | SCENE= }}
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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/hk/1hka_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=1hka 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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BACKGROUND: Folate cofactors are essential for life. Mammals derive folates from their diet, whereas most microorganisms must synthesize folates de novo. Enzymes of the folate pathway therefore provide ideal targets for the development of antimicrobial agents. 6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the transfer of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP), the first reaction in the folate biosynthetic pathway. RESULTS: The crystal structure of HPPK from Escherichia coli has been determined at 1.5 A resolution with a crystallographic R factor of 0.182. The HPPK molecule has a novel three-layered alpha beta alpha fold that creates a valley approximately 26 A long, 10 A wide and 10 A deep. The active center of HPPK is located in the valley and the substrate-binding sites have been identified with the aid of NMR spectroscopy. The HP-binding site is located at one end of the valley, near Asn55, and is sandwiched between two aromatic sidechains. The ATP-binding site is located at the other end of the valley. The adenine base of ATP is positioned near Leu111 and the ribose and the triphosphate extend across and reach the vicinity of HP. CONCLUSIONS: The HPPK structure provides a framework to elucidate structure/function relationships of the enzyme and to analyze mechanisms of pyrophosphoryl transfer. Furthermore, this work may prove useful in the structure-based design of new antimicrobial agents.
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'''6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE'''
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Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents.,Xiao B, Shi G, Chen X, Yan H, Ji X Structure. 1999 May;7(5):489-96. PMID:10378268<ref>PMID:10378268</ref>
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==Overview==
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BACKGROUND: Folate cofactors are essential for life. Mammals derive folates from their diet, whereas most microorganisms must synthesize folates de novo. Enzymes of the folate pathway therefore provide ideal targets for the development of antimicrobial agents. 6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the transfer of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP), the first reaction in the folate biosynthetic pathway. RESULTS: The crystal structure of HPPK from Escherichia coli has been determined at 1.5 A resolution with a crystallographic R factor of 0.182. The HPPK molecule has a novel three-layered alpha beta alpha fold that creates a valley approximately 26 A long, 10 A wide and 10 A deep. The active center of HPPK is located in the valley and the substrate-binding sites have been identified with the aid of NMR spectroscopy. The HP-binding site is located at one end of the valley, near Asn55, and is sandwiched between two aromatic sidechains. The ATP-binding site is located at the other end of the valley. The adenine base of ATP is positioned near Leu111 and the ribose and the triphosphate extend across and reach the vicinity of HP. CONCLUSIONS: The HPPK structure provides a framework to elucidate structure/function relationships of the enzyme and to analyze mechanisms of pyrophosphoryl transfer. Furthermore, this work may prove useful in the structure-based design of new antimicrobial agents.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1HKA 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=1HKA OCA].
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</div>
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<div class="pdbe-citations 1hka" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents., Xiao B, Shi G, Chen X, Yan H, Ji X, Structure. 1999 May;7(5):489-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10378268 10378268]
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*[[HPPK 3D structures|HPPK 3D structures]]
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[[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Chen, X.]]
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[[Category: Chen X]]
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[[Category: Ji, X.]]
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[[Category: Ji X]]
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[[Category: Shi, G.]]
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[[Category: Shi G]]
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[[Category: Xiao, B.]]
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[[Category: Xiao B]]
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[[Category: Yan, H.]]
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[[Category: Yan H]]
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[[Category: 6-hydroxymethyl-7,8-dihydropterin]]
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[[Category: Folate]]
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[[Category: Kinase]]
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[[Category: Pyrophosphokinase]]
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[[Category: Pyrophosphoryl transfer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:56:17 2008''
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Current revision

6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE

PDB ID 1hka

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