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3kkq

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(New page: '''Unreleased structure''' The entry 3kkq is ON HOLD Authors: Muraoka, S., Shima, F., Liao, J., Ijiri, Y., Matsumoto, K., Ye, M., Inoue, T., Kataoka, T. Description: Crystal structure ...)
Current revision (16:13, 1 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3kkq is ON HOLD
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==Crystal structure of M-Ras P40D in complex with GDP==
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<StructureSection load='3kkq' size='340' side='right'caption='[[3kkq]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3kkq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KKQ 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]] 1.2&#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=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3kkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kkq OCA], [https://pdbe.org/3kkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kkq RCSB], [https://www.ebi.ac.uk/pdbsum/3kkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kkq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RASM_MOUSE RASM_MOUSE] May serve as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Weakly activates the MAP kinase pathway (By similarity).
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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/kk/3kkq_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=3kkq 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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Ras family small GTPases assume two interconverting conformations, "inactive" state 1 and "active" state 2, in their GTP-bound forms. Here, to clarify the mechanism of state transition, we have carried out x-ray crystal structure analyses of a series of mutant H-Ras and M-Ras in complex with guanosine 5'-(beta,gamma-imido)triphosphate (GppNHp), representing various intermediate states of the transition. Crystallization of H-RasT35S-GppNHp enables us to solve the first complete tertiary structure of H-Ras state 1 possessing two surface pockets unseen in the state 2 or H-Ras-GDP structure. Moreover, determination of the two distinct crystal structures of H-RasT35S-GppNHp, showing prominent polysterism in the switch I and switch II regions, reveals a pivotal role of the guanine nucleotide-mediated interaction between the two switch regions and its rearrangement by a nucleotide positional change in the state 2 to state 1 transition. Furthermore, the (31)P NMR spectra and crystal structures of the GppNHp-bound forms of M-Ras mutants, carrying various H-Ras-type amino acid substitutions, also reveal the existence of a surface pocket in state 1 and support a similar mechanism based on the nucleotide-mediated interaction and its rearrangement in the state 1 to state 2 transition. Intriguingly, the conformational changes accompanying the state transition mimic those that occurred upon GDP/GTP exchange, indicating a common mechanistic basis inherent in the high flexibility of the switch regions. Collectively, these results clarify the structural features distinguishing the two states and provide new insights into the molecular basis for the state transition of Ras protein.
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Authors: Muraoka, S., Shima, F., Liao, J., Ijiri, Y., Matsumoto, K., Ye, M., Inoue, T., Kataoka, T.
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Structural basis for conformational dynamics of GTP-bound Ras protein.,Shima F, Ijiri Y, Muraoka S, Liao J, Ye M, Araki M, Matsumoto K, Yamamoto N, Sugimoto T, Yoshikawa Y, Kumasaka T, Yamamoto M, Tamura A, Kataoka T J Biol Chem. 2010 Jul 16;285(29):22696-705. Epub 2010 May 17. PMID:20479006<ref>PMID:20479006</ref>
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Description: Crystal structure of M-Ras P40D in complex with GDP
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 18 18:58:02 2009''
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<div class="pdbe-citations 3kkq" 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>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Ijiri Y]]
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[[Category: Inoue T]]
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[[Category: Kataoka T]]
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[[Category: Liao J]]
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[[Category: Matsumoto K]]
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[[Category: Muraoka S]]
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[[Category: Shima F]]
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[[Category: Ye M]]

Current revision

Crystal structure of M-Ras P40D in complex with GDP

PDB ID 3kkq

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