1mrk

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(New page: 200px<br /><applet load="1mrk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mrk, resolution 1.6&Aring;" /> '''STUDIES ON CRYSTAL ST...)
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[[Image:1mrk.gif|left|200px]]<br /><applet load="1mrk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mrk, resolution 1.6&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='1mrk' size='340' side='right'caption='[[1mrk]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1mrk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichosanthes_kirilowii Trichosanthes kirilowii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MRK FirstGlance]. <br>
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1MRK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trichosanthes_kirilowii Trichosanthes kirilowii] 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=1MRK OCA].
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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]] 1.6&#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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==Reference==
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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=1mrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mrk OCA], [https://pdbe.org/1mrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mrk RCSB], [https://www.ebi.ac.uk/pdbsum/1mrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mrk ProSAT]</span></td></tr>
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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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</table>
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[[Category: Single protein]]
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== Function ==
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[https://www.uniprot.org/uniprot/RIPT_TRIKI RIPT_TRIKI] Inactivates eukaryotic 60S ribosomal subunits.
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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/1mrk_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=1mrk ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Trichosanthes kirilowii]]
[[Category: Trichosanthes kirilowii]]
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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 21:39:19 2007''
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Current revision

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

PDB ID 1mrk

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