1mrh: Difference between revisions

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-[[Image:1mrh.gif|left|200px]]
- {{Structure
+==STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS==
-|PDB= 1mrh |SIZE=350|CAPTION= <scene name='initialview01'>1mrh</scene>, resolution 2.0&Aring;
+<StructureSection load='1mrh' size='340' side='right'caption='[[1mrh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=FMC:FORMYCIN'>FMC</scene>
+<table><tr><td colspan='2'>[[1mrh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MRH FirstGlance]. <br>
-|ACTIVITY=
+</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&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMC:(1S)-1-(7-AMINO-1H-PYRAZOLO[4,3-D]PYRIMIDIN-3-YL)-1,4-ANHYDRO-D-RIBITOL'>FMC</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mrh OCA], [https://pdbe.org/1mrh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mrh RCSB], [https://www.ebi.ac.uk/pdbsum/1mrh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mrh ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mrh OCA], [http://www.ebi.ac.uk/pdbsum/1mrh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mrh RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/RIP1_MOMCH RIP1_MOMCH]
+== 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/mr/1mrh_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=1mrh ConSurf].
+<div style="clear:both"></div>
-'''STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS'''
+==See Also==
+*[[Ribosome inactivating protein 3D structures|Ribosome inactivating protein 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Two ribosome-inactivating proteins, trichosanthin and alpha-momorcharin, have been studied in the forms of complexes with ATP or formycin, by an X-ray-crystallographic method at 1.6-2.0 A (0.16-0.20 nm) resolution. The native alpha-momorcharin had been studied at 2.2 A resolution. Structures of trichosanthin were determined by a multiple isomorphous replacement method. Structures of alpha-momorcharin were determined by a molecular replacement method using refined trichosanthin as the searching model. Small ligands in all these complexes have been recognized and built on the difference in electron density. All these structures have been refined to achieve good results, both in terms of crystallography and of ideal geometry. These two proteins show considerable similarity in their three-dimensional folding and to that of related proteins. On the basis of these structures, detailed geometries of the active centres of these two proteins are described and are compared with those of related proteins. In all complexes the interactions between ligand atoms and protein atoms, including hydrophobic forces, aromatic stacking interactions and hydrogen bonds, are found to be specific towards the adenine base. The relationship between the sequence conservation of ribosome-inactivating proteins and their active-centre geometry was analysed. A depurinating mechanism of ribosome-inactivating proteins is proposed on the basis of these results. The N-7 atom of the substrate base group is proposed to be protonated by an acidic residue in the active centre.
+[[Category: Large Structures]]
-==About this Structure==
-MRH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRH OCA].
-==Reference==
-Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins., Huang Q, Liu S, Tang Y, Jin S, Wang Y, Biochem J. 1995 Jul 1;309 ( Pt 1):285-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7619070 7619070]
 [[Category: Momordica charantia]]
-[[Category: Single protein]]
+[[Category: Huang Q]]
-[[Category: Huang, Q.]]
+[[Category: Jin S]]
-[[Category: Jin, S.]]
+[[Category: Liu S]]
-[[Category: Liu, S.]]
+[[Category: Tang Y]]
-[[Category: Tang, Y.]]
+[[Category: Wang Y]]
-[[Category: Wang, Y.]]
-[[Category: ribosome-inactivating protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:11 2008''