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[[Image:2cht.gif|left|200px]]<br /><applet load="2cht" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2cht, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG'''<br />


==Overview==
==CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG==
We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5), the 1.9-A crystal structure of the monofunctional enzyme from Bacillus subtilis. The structure determination process was an unusual one, involving 12 monomers of the enzyme in the asymmetric unit. This structure was solved by the multiple isomorphous replacement method with partial structure phase combination and molecular averaging. The final model, which includes 1380 residues and 522 water molecules in an asymmetric unit, has been refined at 1.9 A and the current crystallographic R value is 0.201. The B. subtilis chorismate mutase is a homotrimer, with beta-sheets from each monomer packing to form the core of a pseudo-alpha beta-barrel with helices on the outside of the trimer. In addition, the active sites have been located by using data from a complex with an endo-oxabicyclic inhibitor that mimics the transition state of the reaction. The structure of this complex has been refined to 2.2 A with a current R value of 0.182 for a model that includes 1388 residues, 12 inhibitor molecules, and 530 water molecules in the asymmetric unit. In each trimer, three equivalent active sites are located at the interfaces of two adjacent subunits.
<StructureSection load='2cht' size='340' side='right'caption='[[2cht]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHT 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]] 2.2&#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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [https://pdbe.org/2cht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [https://www.ebi.ac.uk/pdbsum/2cht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cht ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROH_BACSU AROH_BACSU] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:2105742</ref>
== 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/ch/2cht_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2cht ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2CHT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=TSA:'>TSA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA].
*[[3D structures of chorismate mutase|3D structures of chorismate mutase]]
 
== References ==
==Reference==
<references/>
Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog., Chook YM, Ke H, Lipscomb WN, Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8600-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8378335 8378335]
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Chorismate mutase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Chook YM]]
[[Category: Chook, Y M.]]
[[Category: Ke H]]
[[Category: Ke, H.]]
[[Category: Lipscomb WN]]
[[Category: Lipscomb, W N.]]
[[Category: TSA]]
[[Category: isomerase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:45 2008''

Latest revision as of 12:18, 14 February 2024

CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOGCRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG

Structural highlights

2cht is a 12 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AROH_BACSU Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Gray JV, Golinelli-Pimpaneau B, Knowles JR. Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli. Biochemistry. 1990 Jan 16;29(2):376-83. PMID:2105742

2cht, resolution 2.20Å

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