1hka

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(New page: 200px<br /><applet load="1hka" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hka, resolution 1.50&Aring;" /> '''6-HYDROXYMETHYL-7,8-...)
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[[Image:1hka.jpg|left|200px]]<br /><applet load="1hka" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hka, resolution 1.50&Aring;" />
 
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'''6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE'''<br />
 
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==Overview==
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==6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE==
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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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<StructureSection load='1hka' size='340' side='right'caption='[[1hka]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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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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</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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==About this Structure==
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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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1HKA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HKA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10378268 10378268]
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</div>
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[[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]]
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<div class="pdbe-citations 1hka" style="background-color:#fffaf0;"></div>
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Chen, X.]]
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[[Category: Ji, X.]]
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[[Category: Shi, G.]]
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[[Category: Xiao, B.]]
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[[Category: Yan, H.]]
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[[Category: 6-hydroxymethyl-7]]
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[[Category: 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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:37:19 2007''
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==See Also==
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*[[HPPK 3D structures|HPPK 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Chen X]]
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[[Category: Ji X]]
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[[Category: Shi G]]
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[[Category: Xiao B]]
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[[Category: Yan H]]

Current revision

6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE

PDB ID 1hka

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