3h0v

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{{Seed}}
 
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[[Image:3h0v.png|left|200px]]
 
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==Human AdoMetDC with 5'-Deoxy-5'-(dimethylsulfonio) adenosine==
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The line below this paragraph, containing "STRUCTURE_3h0v", creates the "Structure Box" on the page.
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<StructureSection load='3h0v' size='340' side='right'caption='[[3h0v]], [[Resolution|resolution]] 2.24&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'>[[3h0v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H0V 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]] 2.24&#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=M2T:5-DEOXY-5-(DIMETHYL-LAMBDA~4~-SULFANYL)ADENOSINE'>M2T</scene>, <scene name='pdbligand=PUT:1,4-DIAMINOBUTANE'>PUT</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
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{{STRUCTURE_3h0v| PDB=3h0v | 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=3h0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h0v OCA], [https://pdbe.org/3h0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h0v RCSB], [https://www.ebi.ac.uk/pdbsum/3h0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h0v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DCAM_HUMAN DCAM_HUMAN]
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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/h0/3h0v_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=3h0v 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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S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the polyamine biosynthetic pathway. Inhibition of this pathway and subsequent depletion of polyamine levels is a viable strategy for cancer chemotherapy and for the treatment of parasitic diseases. Substrate analogue inhibitors display an absolute requirement for a positive charge at the position equivalent to the sulfonium of S-adenosylmethionine. We investigated the ligand specificity of AdoMetDC through crystallography, quantum chemical calculations, and stopped-flow experiments. We determined crystal structures of the enzyme cocrystallized with 5'-deoxy-5'-dimethylthioadenosine and 5'-deoxy-5'-(N-dimethyl)amino-8-methyladenosine. The crystal structures revealed a favorable cation-pi interaction between the ligand and the aromatic side chains of Phe7 and Phe223. The estimated stabilization from this interaction is 4.5 kcal/mol as determined by quantum chemical calculations. Stopped-flow kinetic experiments showed that the rate of the substrate binding to the enzyme greatly depends on Phe7 and Phe223, thus supporting the importance of the cation-pi interaction.
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===Human AdoMetDC with 5'-Deoxy-5'-(dimethylsulfonio) adenosine===
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Role of the Sulfonium Center in Determining the Ligand Specificity of Human S-Adenosylmethionine Decarboxylase.,Bale S, Brooks W, Hanes JW, Mahesan AM, Guida WC, Ealick SE Biochemistry. 2009 Jun 15. PMID:19527050<ref>PMID:19527050</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 3h0v" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19527050}}, adds the Publication Abstract to the page
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*[[SAM decarboxylase|SAM decarboxylase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19527050 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19527050}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3H0V is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H0V OCA].
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==Reference==
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<ref group="xtra">PMID:19527050</ref><references group="xtra"/>
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[[Category: Adenosylmethionine decarboxylase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bale, S.]]
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[[Category: Large Structures]]
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[[Category: Ealick, S E.]]
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[[Category: Bale S]]
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[[Category: Guida, W C.]]
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[[Category: Brooks WH]]
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[[Category: Hanes, J W.]]
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[[Category: Ealick SE]]
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[[Category: Mahesan, A M.]]
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[[Category: Guida WC]]
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[[Category: Wesley, B H.]]
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[[Category: Hanes JW]]
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[[Category: Adometdc with competitive substrate analog]]
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[[Category: Mahesan AM]]
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[[Category: Autocatalytic cleavage]]
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[[Category: Decarboxylase]]
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[[Category: Lyase]]
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[[Category: Phosphoprotein]]
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[[Category: Polyamine biosynthesis]]
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[[Category: Pyruvate]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: Schiff base]]
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[[Category: Spermidine biosynthesis]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 22 21:32:03 2009''
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Current revision

Human AdoMetDC with 5'-Deoxy-5'-(dimethylsulfonio) adenosine

PDB ID 3h0v

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