2jas

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[[Image:2jas.gif|left|200px]]
 
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==Structure of deoxyadenosine kinase from M.mycoides with bound dATP==
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The line below this paragraph, containing "STRUCTURE_2jas", creates the "Structure Box" on the page.
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<StructureSection load='2jas' size='340' side='right'caption='[[2jas]], [[Resolution|resolution]] 2.70&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'>[[2jas]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma_mycoides_subsp._mycoides_SC Mycoplasma mycoides subsp. mycoides SC]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JAS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_2jas| PDB=2jas | SCENE= }}
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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=2jas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jas OCA], [https://pdbe.org/2jas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jas RCSB], [https://www.ebi.ac.uk/pdbsum/2jas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jas ProSAT]</span></td></tr>
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</table>
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'''STRUCTURE OF DEOXYADENOSINE KINASE FROM M.MYCOIDES WITH BOUND DATP'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q93IG4_MYCMI Q93IG4_MYCMI]
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== Evolutionary Conservation ==
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==Overview==
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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/ja/2jas_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=2jas 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 ==
Deoxyribonucleoside kinases (dNKs) catalyze the transfer of a phosphoryl group from ATP to a deoxyribonucleoside (dN), a key step in DNA precursor synthesis. Recently structural information concerning dNKs has been obtained, but no structure of a bacterial dCK/dGK enzyme is known. Here we report the structure of such an enzyme, represented by deoxyadenosine kinase from Mycoplasma mycoides subsp. mycoides small colony type (Mm-dAK). Superposition of Mm-dAK with its human counterpart's deoxyguanosine kinase (dGK) and deoxycytidine kinase (dCK) reveals that the overall structures are very similar with a few amino acid alterations in the proximity of the active site. To investigate the substrate specificity, Mm-dAK has been crystallized in complex with dATP and dCTP, as well as the products dCMP and dCDP. Both dATP and dCTP bind to the enzyme in a feedback-inhibitory manner with the dN part in the deoxyribonucleoside binding site and the triphosphates in the P-loop. Substrate specificity studies with clinically important nucleoside analogs as well as several phosphate donors were performed. Thus, in this study we combine structural and kinetic data to gain a better understanding of the substrate specificity of the dCK/dGK family of enzymes. The structure of Mm-dAK provides a starting point for making new anti bacterial agents against pathogenic bacteria.
Deoxyribonucleoside kinases (dNKs) catalyze the transfer of a phosphoryl group from ATP to a deoxyribonucleoside (dN), a key step in DNA precursor synthesis. Recently structural information concerning dNKs has been obtained, but no structure of a bacterial dCK/dGK enzyme is known. Here we report the structure of such an enzyme, represented by deoxyadenosine kinase from Mycoplasma mycoides subsp. mycoides small colony type (Mm-dAK). Superposition of Mm-dAK with its human counterpart's deoxyguanosine kinase (dGK) and deoxycytidine kinase (dCK) reveals that the overall structures are very similar with a few amino acid alterations in the proximity of the active site. To investigate the substrate specificity, Mm-dAK has been crystallized in complex with dATP and dCTP, as well as the products dCMP and dCDP. Both dATP and dCTP bind to the enzyme in a feedback-inhibitory manner with the dN part in the deoxyribonucleoside binding site and the triphosphates in the P-loop. Substrate specificity studies with clinically important nucleoside analogs as well as several phosphate donors were performed. Thus, in this study we combine structural and kinetic data to gain a better understanding of the substrate specificity of the dCK/dGK family of enzymes. The structure of Mm-dAK provides a starting point for making new anti bacterial agents against pathogenic bacteria.
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==About this Structure==
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Structure-function analysis of a bacterial deoxyadenosine kinase reveals the basis for substrate specificity.,Welin M, Wang L, Eriksson S, Eklund H J Mol Biol. 2007 Mar 9;366(5):1615-23. Epub 2006 Dec 8. PMID:17229440<ref>PMID:17229440</ref>
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2JAS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_mycoides_subsp._mycoides_sc Mycoplasma mycoides subsp. mycoides sc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAS 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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Structure-function analysis of a bacterial deoxyadenosine kinase reveals the basis for substrate specificity., Welin M, Wang L, Eriksson S, Eklund H, J Mol Biol. 2007 Mar 9;366(5):1615-23. Epub 2006 Dec 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17229440 17229440]
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</div>
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[[Category: Deoxyguanosine kinase]]
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<div class="pdbe-citations 2jas" style="background-color:#fffaf0;"></div>
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[[Category: Mycoplasma mycoides subsp. mycoides sc]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Eklund, H.]]
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__TOC__
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[[Category: Eriksson, S.]]
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</StructureSection>
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[[Category: Wang, L.]]
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[[Category: Large Structures]]
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[[Category: Welin, M.]]
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[[Category: Mycoplasma mycoides subsp. mycoides SC]]
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[[Category: Deoxyribonucleoside kinase]]
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[[Category: Eklund H]]
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[[Category: Kinase]]
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[[Category: Eriksson S]]
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[[Category: Transferase]]
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[[Category: Wang L]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:37:18 2008''
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[[Category: Welin M]]

Current revision

Structure of deoxyadenosine kinase from M.mycoides with bound dATP

PDB ID 2jas

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