1fig: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1fig.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1fig", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1fig|  PDB=1fig  |  SCENE=  }}
'''ROUTES TO CATALYSIS: STRUCTURE OF A CATALYTIC ANTIBODY AND COMPARISON WITH ITS NATURAL COUNTERPART'''


==ROUTES TO CATALYSIS: STRUCTURE OF A CATALYTIC ANTIBODY AND COMPARISON WITH ITS NATURAL COUNTERPART==
<StructureSection load='1fig' size='340' side='right'caption='[[1fig]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/1fig_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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:8303271<ref>PMID:8303271</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1FIG is a [[Protein complex]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FIG OCA].
</div>
<div class="pdbe-citations 1fig" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/8303271 8303271]
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
[[Category: Protein complex]]
== References ==
[[Category: Haynes, M R.]]
<references/>
[[Category: Hilvert, D.]]
__TOC__
[[Category: Stura, E A.]]
</StructureSection>
[[Category: Wilson, I A.]]
[[Category: Large Structures]]
[[Category: Immunoglobulin]]
[[Category: Mus musculus]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:22:02 2008''
[[Category: Haynes MR]]
[[Category: Hilvert D]]
[[Category: Stura EA]]
[[Category: Wilson IA]]