1mrh

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(New page: 200px<br /><applet load="1mrh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mrh, resolution 2.0&Aring;" /> '''STUDIES ON CRYSTAL ST...)
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[[Image:1mrh.gif|left|200px]]<br /><applet load="1mrh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mrh, resolution 2.0&Aring;" />
 
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'''STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS'''<br />
 
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==Overview==
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==STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS==
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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.
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<StructureSection load='1mrh' size='340' side='right'caption='[[1mrh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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&#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=FMC:(1S)-1-(7-AMINO-1H-PYRAZOLO[4,3-D]PYRIMIDIN-3-YL)-1,4-ANHYDRO-D-RIBITOL'>FMC</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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RIP1_MOMCH RIP1_MOMCH]
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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/mr/1mrh_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=1mrh 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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1MRH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia] with FMC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MRH OCA].
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*[[Ribosome inactivating protein 3D structures|Ribosome inactivating protein 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7619070 7619070]
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[[Category: Large Structures]]
[[Category: Momordica charantia]]
[[Category: Momordica charantia]]
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[[Category: Single protein]]
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[[Category: Huang Q]]
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[[Category: Huang, Q.]]
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[[Category: Jin S]]
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[[Category: Jin, S.]]
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[[Category: Liu S]]
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[[Category: Liu, S.]]
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[[Category: Tang Y]]
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[[Category: Tang, Y.]]
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[[Category: Wang Y]]
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[[Category: Wang, Y.]]
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[[Category: FMC]]
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[[Category: ribosome-inactivating protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:39:09 2007''
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Current revision

STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS

PDB ID 1mrh

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