2ada

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(New page: 200px<br /><applet load="2ada" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ada, resolution 2.4&Aring;" /> '''ATOMIC STRUCTURE OF A...)
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[[Image:2ada.gif|left|200px]]<br /><applet load="2ada" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ada, resolution 2.4&Aring;" />
 
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'''ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS'''<br />
 
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==Overview==
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==ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS==
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The crystal structure of a murine adenosine deaminase complexed with, 6-hydroxyl-1,6-dihydropurine ribonucleoside, a nearly ideal, transition-state analog, has been determined and refined at 2.4 angstrom, resolution. The structure is folded as an eight-stranded parallel, alpha/beta barrel with a deep pocket at the beta-barrel COOH-terminal end, wherein the inhibitor and a zinc are bound and completely sequestered. The, presence of the zinc cofactor and the precise structure of the bound, analog were not previously known. The 6R isomer of the analog is very, tightly held in place by the coordination of the 6-hydroxyl to the zinc, and the formation of nine hydrogen bonds. On the basis of the structure of, the complex a stereoselective addition-elimination or SN2 mechanism of the, enzyme is proposed with the zinc atom and the Glu and Asp residues playing, key roles. A molecular explanation of a hereditary disease caused by, several point mutations of an enzyme is also presented.
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<StructureSection load='2ada' size='340' side='right'caption='[[2ada]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADA FirstGlance]. <br>
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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]] 2.4&#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=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [https://pdbe.org/2ada PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [https://www.ebi.ac.uk/pdbsum/2ada PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ada ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADA_MOUSE ADA_MOUSE] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).
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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/ad/2ada_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=2ada ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2ADA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN and HPR as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1ADA. Active as [http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA].
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*[[Adenosine deaminase 3D structures|Adenosine deaminase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations., Wilson DK, Rudolph FB, Quiocho FA, Science. 1991 May 31;252(5010):1278-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1925539 1925539]
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[[Category: Large Structures]]
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[[Category: Adenosine deaminase]]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Quiocho FA]]
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[[Category: Quiocho, F.A.]]
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[[Category: Wilson DK]]
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[[Category: Wilson, D.K.]]
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[[Category: HPR]]
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[[Category: ZN]]
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[[Category: hydrolase (amino)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:03:45 2007''
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ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS

PDB ID 2ada

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