2mas: Difference between revisions

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-{{Seed}}
-[[Image:2mas.png|left|200px]]
-<!--
+==PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR==
-The line below this paragraph, containing "STRUCTURE_2mas", creates the "Structure Box" on the page.
+<StructureSection load='2mas' size='340' side='right'caption='[[2mas]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<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>
-{{STRUCTURE_2mas|  PDB=2mas  |  SCENE=  }}
+<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>
+</table>
+== Function ==
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/2mas_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_9572842}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2mas" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 9572842 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9572842}}
+__TOC__
+</StructureSection>
-==About this Structure==
-MAS is a [[Single protein]] structure of sequence from [http://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].
-==Reference==
-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://www.ncbi.nlm.nih.gov/pubmed/9572842 9572842]
 [[Category: Crithidia fasciculata]]
-[[Category: Purine nucleosidase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Degano M]]
-[[Category: Degano, M.]]
+[[Category: Sacchettini JC]]
-[[Category: Sacchettini, J C.]]
+[[Category: Schramm VL]]
-[[Category: Schramm, V L.]]
-[[Category: Hydrolase]]
-[[Category: Inosine]]
-[[Category: Iu-nh]]
-[[Category: Purine nucleosidase]]
-[[Category: Purine nucleoside hydrolase]]
-[[Category: Uridine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:27:24 2008''