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1fig

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(New page: 200px<br /> <applet load="1fig" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fig, resolution 3.0&Aring;" /> '''ROUTES TO CATALYSIS:...)
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[[Image:1fig.gif|left|200px]]<br />
 
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<applet load="1fig" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fig, resolution 3.0&Aring;" />
 
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'''ROUTES TO CATALYSIS: STRUCTURE OF A CATALYTIC ANTIBODY AND COMPARISON WITH ITS NATURAL COUNTERPART'''<br />
 
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==Overview==
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==ROUTES TO CATALYSIS: STRUCTURE OF A CATALYTIC ANTIBODY AND COMPARISON WITH ITS NATURAL COUNTERPART==
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The three-dimensional structure of a catalytic antibody (1F7) with, chorismate mutase activity has been determined to 3.0 A resolution as a, complex with a transition state analog. The structural data suggest that, the antibody stabilizes the same conformationally restricted pericyclic, transition state as occurs in the uncatalyzed reaction. Overall shape and, charge complementarity between the combining site and the transition state, analog dictate preferential binding of the correct substrate enantiomer in, a conformation appropriate for reaction. Comparison with the structure of, a chorismate mutase enzyme indicates an overall similarity between the, catalytic mechanism employed by the two proteins. Differences in the, number of specific interactions available for restricting the rotational, degrees of freedom in the transition state, and the lack of multiple, electrostatic interactions that might stabilize charge separation in this, highly polarized metastable species, are likely to account for the, observed 10(4) times lower activity of the antibody relative to that of, the natural enzymes that catalyze this reaction. The structure of the 1F7, Fab'-hapten complex provides confirmation that the properties of an, antibody catalyst faithfully reflect the design of the transition state, analog.
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<StructureSection load='1fig' size='340' side='right'caption='[[1fig]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fig]] is a 2 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=1FIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FIG 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]] 3&#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=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</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=1fig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fig OCA], [https://pdbe.org/1fig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fig RCSB], [https://www.ebi.ac.uk/pdbsum/1fig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fig ProSAT]</span></td></tr>
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</table>
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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/fi/1fig_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=1fig 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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1FIG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with TSA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FIG OCA].
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Routes to catalysis: structure of a catalytic antibody and comparison with its natural counterpart., Haynes MR, Stura EA, Hilvert D, Wilson IA, Science. 1994 Feb 4;263(5147):646-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8303271 8303271]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Mus musculus]]
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[[Category: Haynes, M.R.]]
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[[Category: Haynes MR]]
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[[Category: Hilvert, D.]]
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[[Category: Hilvert D]]
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[[Category: Stura, E.A.]]
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[[Category: Stura EA]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson IA]]
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[[Category: TSA]]
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[[Category: immunoglobulin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:30:15 2007''
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Current revision

ROUTES TO CATALYSIS: STRUCTURE OF A CATALYTIC ANTIBODY AND COMPARISON WITH ITS NATURAL COUNTERPART

PDB ID 1fig

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