3km3

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==Crystal structure of eoxycytidine triphosphate deaminase from anaplasma phagocytophilum at 2.1A resolution==
==Crystal structure of eoxycytidine triphosphate deaminase from anaplasma phagocytophilum at 2.1A resolution==
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<StructureSection load='3km3' size='340' side='right' caption='[[3km3]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='3km3' size='340' side='right'caption='[[3km3]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3km3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anapz Anapz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KM3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3km3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anaplasma_phagocytophilum_str._HZ Anaplasma phagocytophilum str. HZ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KM3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
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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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k9g|3k9g]], [[3kw3|3kw3]], [[3luz|3luz]], [[3men|3men]], [[3njb|3njb]], [[3o2e|3o2e]], [[3oib|3oib]], [[3p96|3p96]], [[3pfd|3pfd]], [[3pm6|3pm6]]</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=IOD:IODIDE+ION'>IOD</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dcd, APH_0130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=212042 ANAPZ])</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=3km3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3km3 OCA], [https://pdbe.org/3km3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3km3 RCSB], [https://www.ebi.ac.uk/pdbsum/3km3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3km3 ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dCTP_deaminase dCTP deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.13 3.5.4.13] </span></td></tr>
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<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=3km3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3km3 OCA], [http://pdbe.org/3km3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3km3 RCSB], [http://www.ebi.ac.uk/pdbsum/3km3 PDBsum]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DCD_ANAPZ DCD_ANAPZ]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/3km3_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/3km3_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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</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=3km3 ConSurf].
</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=3km3 ConSurf].
<div style="clear:both"></div>
<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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The Seattle Structural Genomics Center for Infectious Disease (SSGCID) focuses on the structure elucidation of potential drug targets from class A, B, and C infectious disease organisms. Many SSGCID targets are selected because they have homologs in other organisms that are validated drug targets with known structures. Thus, many SSGCID targets are expected to be solved by molecular replacement (MR), and reflective of this, all proteins are expressed in native form. However, many community request targets do not have homologs with known structures and not all internally selected targets readily solve by MR, necessitating experimental phase determination. We have adopted the use of iodide ion soaks and single wavelength anomalous dispersion (SAD) experiments as our primary method for de novo phasing. This method uses existing native crystals and in house data collection, resulting in rapid, low cost structure determination. Iodide ions are non-toxic and soluble at molar concentrations, facilitating binding at numerous hydrophobic or positively charged sites. We have used this technique across a wide range of crystallization conditions with successful structure determination in 16 of 17 cases within the first year of use (94% success rate). Here we present a general overview of this method as well as several examples including SAD phasing of proteins with novel folds and the combined use of SAD and MR for targets with weak MR solutions. These cases highlight the straightforward and powerful method of iodide ion SAD phasing in a high-throughput structural genomics environment.
 
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SAD phasing using iodide ions in a high-throughput structural genomics environment.,Abendroth J, Gardberg AS, Robinson JI, Christensen JS, Staker BL, Myler PJ, Stewart LJ, Edwards TE J Struct Funct Genomics. 2011 Jul;12(2):83-95. Epub 2011 Feb 27. PMID:21359836<ref>PMID:21359836</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 3km3" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Deaminase|Deaminase]]
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*[[Deaminase 3D structures|Deaminase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Anapz]]
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[[Category: Anaplasma phagocytophilum str. HZ]]
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[[Category: DCTP deaminase]]
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[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Anaplasma phagocytophilum]]
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[[Category: Decode]]
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[[Category: Deoxycytidine triphosphate deaminase]]
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[[Category: Hydrolase]]
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[[Category: Iodide phasing]]
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[[Category: Niaid]]
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[[Category: Nih]]
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[[Category: Nucleotide metabolism]]
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[[Category: Sbri]]
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[[Category: Ssgcid]]
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[[Category: Uw]]
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Current revision

Crystal structure of eoxycytidine triphosphate deaminase from anaplasma phagocytophilum at 2.1A resolution

PDB ID 3km3

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