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2mas

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(New page: 200px<br /> <applet load="2mas" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mas, resolution 2.3&Aring;" /> '''PURINE NUCLEOSIDE HY...)
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[[Image:2mas.gif|left|200px]]<br />
 
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<applet load="2mas" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2mas, resolution 2.3&Aring;" />
 
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'''PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR'''<br />
 
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==Overview==
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==PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR==
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Nucleoside N-ribohydrolases are targets for disruption of purine salvage, in the protozoan parasites. The structure of a trypanosomal, N-ribohydrolase in complex with a transition-state inhibitor is reported, at 2.3 A resolution. The nonspecific nucleoside hydrolase from Crithidia, fasciculata cocrystallized with p-aminophenyliminoribitol reveals tightly, bound Ca2+ as a catalytic site ligand. The complex with the, transition-state inhibitor is characterized by (1) large protein, conformational changes to create a hydrophobic leaving group site (2), C3'-exo geometry for the inhibitor, typical of a ribooxocarbenium ion (3), stabilization of the ribooxocarbenium analogue between the neighboring, group 5'-hydroxyl and bidentate hydrogen bonds to Asn168; and (4), octacoordinate Ca2+ orients a ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9572842 (full description)]]
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<StructureSection load='2mas' size='340' side='right'caption='[[2mas]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2mas]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAS 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]] 2.3&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PIR:2-(4-AMINO-PHENYL)-5-HYDROXYMETHYL-PYRROLIDINE-3,4-DIOL'>PIR</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=2mas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mas OCA], [https://pdbe.org/2mas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mas RCSB], [https://www.ebi.ac.uk/pdbsum/2mas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mas ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IUNH_CRIFA IUNH_CRIFA] Catalyzes the hydrolysis of all of the commonly occurring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates.
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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/ma/2mas_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=2mas 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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Nucleoside N-ribohydrolases are targets for disruption of purine salvage in the protozoan parasites. The structure of a trypanosomal N-ribohydrolase in complex with a transition-state inhibitor is reported at 2.3 A resolution. The nonspecific nucleoside hydrolase from Crithidia fasciculata cocrystallized with p-aminophenyliminoribitol reveals tightly bound Ca2+ as a catalytic site ligand. The complex with the transition-state inhibitor is characterized by (1) large protein conformational changes to create a hydrophobic leaving group site (2) C3'-exo geometry for the inhibitor, typical of a ribooxocarbenium ion (3) stabilization of the ribooxocarbenium analogue between the neighboring group 5'-hydroxyl and bidentate hydrogen bonds to Asn168; and (4) octacoordinate Ca2+ orients a catalytic site water and is liganded to two hydroxyls of the inhibitor. The mechanism is ribooxocarbenium stabilization with weak leaving group activation and is a departure from glucohydrolases which use paired carboxylates to achieve the transition state.
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==About this Structure==
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Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor.,Degano M, Almo SC, Sacchettini JC, Schramm VL Biochemistry. 1998 May 5;37(18):6277-85. PMID:9572842<ref>PMID:9572842</ref>
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2MAS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]] with CA and PIR as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.1 3.2.2.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2MAS 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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Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor., Degano M, Almo SC, Sacchettini JC, Schramm VL, Biochemistry. 1998 May 5;37(18):6277-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9572842 9572842]
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</div>
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<div class="pdbe-citations 2mas" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Crithidia fasciculata]]
[[Category: Crithidia fasciculata]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Degano, M.]]
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[[Category: Degano M]]
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[[Category: Sacchettini, J.C.]]
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[[Category: Sacchettini JC]]
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[[Category: Schramm, V.L.]]
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[[Category: Schramm VL]]
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[[Category: CA]]
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[[Category: PIR]]
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[[Category: hydrolase]]
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[[Category: inosine]]
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[[Category: iu-nh]]
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[[Category: purine nucleosidase]]
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[[Category: purine nucleoside hydrolase]]
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[[Category: uridine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:52:47 2007''
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Current revision

PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR

PDB ID 2mas

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