1dgm

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[[Image:1dgm.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF ADENOSINE KINASE FROM TOXOPLASMA GONDII==
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|PDB= 1dgm |SIZE=350|CAPTION= <scene name='initialview01'>1dgm</scene>, resolution 1.80&Aring;
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<StructureSection load='1dgm' size='340' side='right'caption='[[1dgm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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<table><tr><td colspan='2'>[[1dgm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DGM FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </span>
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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]] 1.8&#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=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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|DOMAIN=
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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=1dgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgm OCA], [https://pdbe.org/1dgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dgm RCSB], [https://www.ebi.ac.uk/pdbsum/1dgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dgm ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgm OCA], [http://www.ebi.ac.uk/pdbsum/1dgm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dgm RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/ADK_TOXGO ADK_TOXGO] ATP-dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. It is a key purine metabolic enzyme in the opportunistic parasitic protozoan toxoplasma gondii as it cannot synthesize purines de novo.
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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/dg/1dgm_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=1dgm 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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Human infection with Toxoplasma gondii is an important cause of morbidity and mortality. Protozoan parasites such as T. gondii are incapable of de novo purine biosynthesis and must acquire purines from their host, so the purine salvage pathway offers a number of potential targets for antiparasitic chemotherapy. In T. gondii tachyzoites, adenosine is the predominantly salvaged purine nucleoside, and thus adenosine kinase is a key enzyme in the purine salvage pathway of this parasite. The structure of T. gondii adenosine kinase was solved using molecular replacement and refined by simulated annealing at 1.8 A resolution to an R-factor of 0.214. The overall structure and the active site geometry are similar to human adenosine kinase, although there are significant differences. The T. gondii adenosine kinase has several unique features compared to the human sequence, including a five-residue deletion in one of the four linking segments between the two domains, which is probably responsible for a major change in the orientation of the two domains with respect to each other. These structural differences suggest the possibility of developing specific inhibitors of the parasitic enzyme.
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'''CRYSTAL STRUCTURE OF ADENOSINE KINASE FROM TOXOPLASMA GONDII'''
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Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution.,Cook WJ, DeLucas LJ, Chattopadhyay D Protein Sci. 2000 Apr;9(4):704-12. PMID:10794412<ref>PMID:10794412</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 1dgm" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Human infection with Toxoplasma gondii is an important cause of morbidity and mortality. Protozoan parasites such as T. gondii are incapable of de novo purine biosynthesis and must acquire purines from their host, so the purine salvage pathway offers a number of potential targets for antiparasitic chemotherapy. In T. gondii tachyzoites, adenosine is the predominantly salvaged purine nucleoside, and thus adenosine kinase is a key enzyme in the purine salvage pathway of this parasite. The structure of T. gondii adenosine kinase was solved using molecular replacement and refined by simulated annealing at 1.8 A resolution to an R-factor of 0.214. The overall structure and the active site geometry are similar to human adenosine kinase, although there are significant differences. The T. gondii adenosine kinase has several unique features compared to the human sequence, including a five-residue deletion in one of the four linking segments between the two domains, which is probably responsible for a major change in the orientation of the two domains with respect to each other. These structural differences suggest the possibility of developing specific inhibitors of the parasitic enzyme.
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*[[Adenosine kinase 3D structures|Adenosine kinase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1DGM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGM OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution., Cook WJ, DeLucas LJ, Chattopadhyay D, Protein Sci. 2000 Apr;9(4):704-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10794412 10794412]
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[[Category: Adenosine kinase]]
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[[Category: Single protein]]
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[[Category: Toxoplasma gondii]]
[[Category: Toxoplasma gondii]]
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[[Category: Chattopadhyay, D.]]
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[[Category: Chattopadhyay D]]
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[[Category: Cook, W J.]]
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[[Category: Cook WJ]]
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[[Category: DeLucas, L J.]]
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[[Category: DeLucas LJ]]
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[[Category: adenosine kinase]]
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[[Category: purine metabolism]]
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[[Category: toxoplasma gondii]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:41:21 2008''
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Current revision

CRYSTAL STRUCTURE OF ADENOSINE KINASE FROM TOXOPLASMA GONDII

PDB ID 1dgm

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