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1mit

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(New page: 200px<br /><applet load="1mit" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mit" /> '''RECOMBINANT CUCURBITA MAXIMA TRYPSIN INHIBIT...)
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[[Image:1mit.gif|left|200px]]<br /><applet load="1mit" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mit" />
 
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'''RECOMBINANT CUCURBITA MAXIMA TRYPSIN INHIBITOR V (RCMTI-V) (NMR, MINIMIZED AVERAGE STRUCTURE)'''<br />
 
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==Overview==
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==RECOMBINANT CUCURBITA MAXIMA TRYPSIN INHIBITOR V (RCMTI-V) (NMR, MINIMIZED AVERAGE STRUCTURE)==
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The solution structure of recombinant Cucurbita maxima trypsin inhibitor-V, (rCMTI-V), whose N-terminal is unacetylated and carries an extra glycine, residue, was determined by means of two-dimensional (2D) homo and 3D, hetero NMR experiments in combination with a distance geometry and, simulated annealing algorithm. A total of 927 interproton distances and, 123 torsion angle constraints were utilized to generate 18 structures. The, root mean squared deviation (RMSD) of the mean structure is 0.53 A for, main-chain atoms and 0.95 A for all the non-hydrogen atoms of residues, 3-40 and 49-67. The average structure of rCMTI-V is found to be almost the, same as that of the native protein [Cai, M., Gong, Y., Kao, J.-L., &amp;, Krishnamoorthi, R. (1995) Biochemistry 34, 5201-5211]. The backbone, dynamics of uniformly 15N-labeled rCMTI-V were characterized by 2D 1H-15N, NMR methods. 15N spin-lattice and spin-spin relaxation rate constants (R1, and R2, respectively) and [1H]-15N steady-state heteronuclear Overhauser, effect enhancements were measured for the peptide NH units and, using the, model-free formalism [Lipari, G., &amp; Szabo, A. (1982) J. Am. Chem. Soc., 104, 4546-4559, 4559-4570], the following parameters were determined:, overall tumbling correlation time for the protein molecule (tau m), generalized order parameters for the individual N-H vectors (S2), effective correlation times for their internal motions (tau e), and terms, to account for motions on a slower time scale (second) due to chemical, exchange and/or conformational averaging (R(ex)). Most of the backbone NH, groups of rCMTI-V are found to be highly constrained ((S2) = 0.83) with, the exception of those in the binding loop (residues 41-48, (S2) = 0.71), and the N-terminal region ((S2) = 0.73). Main-chain atoms in these regions, show large RMSD values in the average NMR structure. Residues involved in, turns also appear to have more mobility ((S2) = 0.80). Dynamical, properties of rCMTI-V were compared with those of two other inhibitors of, the potato I family--eglin c [Peng, J. W., &amp; Wagner, G. (1992), Biochemistry 31, 8571-8586] and barley chymotrypsin inhibitor 2 [CI-2;, Shaw, G. L., Davis, B., Keeler, J., &amp; Fersht, A. R. (1995) Biochemistry, 34, 2225-2233]. The Cys3-Cys48 linkage found only in rCMTI-V appears to, somewhat reduce the N-terminal flexibility; likewise, the C-terminal of, rCMTI-V, being part of a beta-sheet, appears to be more rigid.
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<StructureSection load='1mit' size='340' side='right'caption='[[1mit]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mit]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MIT 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">Solution NMR</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=1mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mit OCA], [https://pdbe.org/1mit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mit RCSB], [https://www.ebi.ac.uk/pdbsum/1mit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mit ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ITH5_CUCMA ITH5_CUCMA] Specifically inhibits both trypsin and activated Hageman factor.
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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/mi/1mit_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=1mit 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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1MIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MIT OCA].
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*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy., Liu J, Prakash O, Cai M, Gong Y, Huang Y, Wen L, Wen JJ, Huang JK, Krishnamoorthi R, Biochemistry. 1996 Feb 6;35(5):1516-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8634282 8634282]
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[[Category: Cucurbita maxima]]
[[Category: Cucurbita maxima]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cai, M.]]
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[[Category: Cai M]]
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[[Category: Gong, Y.]]
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[[Category: Gong Y]]
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[[Category: Huang, J.K.]]
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[[Category: Huang J-K]]
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[[Category: Huang, Y.]]
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[[Category: Huang Y]]
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[[Category: Krishnamoorthi, R.]]
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[[Category: Krishnamoorthi R]]
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[[Category: Liu, J.]]
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[[Category: Liu J]]
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[[Category: Prakash, O.]]
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[[Category: Prakash O]]
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[[Category: Wen, J.J.]]
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[[Category: Wen JJ]]
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[[Category: Wen, L.]]
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[[Category: Wen L]]
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[[Category: serine protease inhibitor (rcmti-v)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:26:28 2007''
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Current revision

RECOMBINANT CUCURBITA MAXIMA TRYPSIN INHIBITOR V (RCMTI-V) (NMR, MINIMIZED AVERAGE STRUCTURE)

PDB ID 1mit

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