1com: Difference between revisions

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{{Seed}}
[[Image:1com.png|left|200px]]


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==THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION==
The line below this paragraph, containing "STRUCTURE_1com", creates the "Structure Box" on the page.
<StructureSection load='1com' size='340' side='right'caption='[[1com]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1com]] 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=1COM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COM FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRE:PREPHENIC+ACID'>PRE</scene></td></tr>
{{STRUCTURE_1com| PDB=1com |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1com FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1com OCA], [https://pdbe.org/1com PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1com RCSB], [https://www.ebi.ac.uk/pdbsum/1com PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1com 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/co/1com_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=1com ConSurf].
<div style="clear:both"></div>


===THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION===
==See Also==
 
*[[3D structures of chorismate mutase|3D structures of chorismate mutase]]
 
== References ==
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(as it appears on PubMed at http://www.pubmed.gov), where 8046752 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8046752}}
 
==About this Structure==
1COM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COM OCA].
 
==Reference==
The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction., Chook YM, Gray JV, Ke H, Lipscomb WN, J Mol Biol. 1994 Jul 29;240(5):476-500. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8046752 8046752]
[[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: Chorismate mutase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:01:44 2008''

Latest revision as of 09:44, 7 February 2024

THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTIONTHE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION

Structural highlights

1com 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

1com, resolution 2.20Å

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