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| | ==CRYSTAL STRUCTURE OF UNLIGATED HPPK(R92A) FROM E.COLI AT 1.55 ANGSTROM RESOLUTION== | | ==CRYSTAL STRUCTURE OF UNLIGATED HPPK(R92A) FROM E.COLI AT 1.55 ANGSTROM RESOLUTION== |
| - | <StructureSection load='1kbr' size='340' side='right' caption='[[1kbr]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='1kbr' size='340' side='right'caption='[[1kbr]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kbr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KBR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kbr]] 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=1KBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KBR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hka|1hka]], [[1eqm|1eqm]], [[1eq0|1eq0]], [[1eqo|1eqo]], [[1ex8|1ex8]], [[1cbk|1cbk]], [[1dy3|1dy3]], [[1f9y|1f9y]], [[1f9h|1f9h]], [[1g4c|1g4c]], [[1hq2|1hq2]], [[1hq9|1hq9]], [[1im6|1im6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kbr OCA], [https://pdbe.org/1kbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kbr RCSB], [https://www.ebi.ac.uk/pdbsum/1kbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kbr ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kbr OCA], [http://pdbe.org/1kbr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kbr RCSB], [http://www.ebi.ac.uk/pdbsum/1kbr PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HPPK_ECOLI HPPK_ECOLI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/1kbr_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/1kbr_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | ==See Also== | | ==See Also== |
| - | *[[6-hydroxymethyl-7%2C8-dihydropterin pyrophosphokinase|6-hydroxymethyl-7%2C8-dihydropterin pyrophosphokinase]] | + | *[[HPPK 3D structures|HPPK 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Blaszczyk, J]] | + | [[Category: Blaszczyk J]] |
| - | [[Category: Ji, X]] | + | [[Category: Ji X]] |
| - | [[Category: 6-hydroxymethyl-7]]
| + | |
| - | [[Category: 8-dihydropterin]]
| + | |
| - | [[Category: Antimicrobial agent]]
| + | |
| - | [[Category: Drug design]]
| + | |
| - | [[Category: Folate]]
| + | |
| - | [[Category: Hppk]]
| + | |
| - | [[Category: Pterin]]
| + | |
| - | [[Category: Pyrophosphokinase]]
| + | |
| - | [[Category: Pyrophosphoryl transfer]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
HPPK_ECOLI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP), the first reaction in the folate biosynthetic pathway. Arginine residues 82 and 92, strictly conserved in 35 HPPK sequences, play dynamic roles in the catalytic cycle of the enzyme. At 0.89-A resolution, two distinct conformations are observed for each of the two residues in the crystal structure of the wild-type HPPK in complex with two HP variants, two Mg(2+) ions, and an ATP analogue. Structural information suggests that R92 first binds to the alpha-phosphate group of ATP and then shifts to interact with the beta-phosphate as R82, which initially does not bind to ATP, moves in and binds to alpha-phosphate when the pyrophosphoryl transfer is about to occur. The dynamic roles of R82 and R92 are further elucidated by five more crystal structures of two mutant proteins, R82A and R92A, with and without bound ligands. Two oxidized forms of HP are observed with an occupancy ratio of 0.50:0.50 in the 0.89-A structure. The oxidation of HP has significant impact on its binding to the protein as well as the conformation of nearby residue W89.
Dynamic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: crystallographic studies.,Blaszczyk J, Li Y, Shi G, Yan H, Ji X Biochemistry. 2003 Feb 18;42(6):1573-80. PMID:12578370[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Blaszczyk J, Li Y, Shi G, Yan H, Ji X. Dynamic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: crystallographic studies. Biochemistry. 2003 Feb 18;42(6):1573-80. PMID:12578370 doi:10.1021/bi0267994
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