Chorismate mutase: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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+<StructureSection load='2fp2' size='340' side='right' caption='Bacillus subtilis chorismate mutase complex with transition state analog (PDB code [[2fp2]]).' scene='91/916399/Cv/1'>
-<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
 == Function ==
-'''Chorismate mutase'''.(CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr . CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>..  CHM is divided to 2 classes: AroH class which is monofunctional and th bifunctional AroQ.
+'''Chorismate mutase''' (CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr. CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>. CHM is divided into 2 classes: '''AroH''' class which is monofunctional and the bifunctional '''AroQ'''.
+*'''Bifunctional chorismate mutase/hexadienyl dehydratase''' catalyze 2 subsequent reactions in the biosynthesis of Phe<ref>PMID:37586588</ref>.
-== Disease ==
+== Relevance ==
-== Relevance ==
+CHM belongs to the aromatic acids biogenesis pathway in prokaryotes which differs from that of humans. Hence, the presence of CHM indicates the presence of virulent bacteria and its detection is used in developing rational therapeutics against bacterial virulence<ref>PMID:29717997</ref>.
 == Structural highlights ==
-This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
+The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The <scene name='91/916399/Cv/4'>transition state analog is buried in the active site pocket and forms extensive H-bond network</scene> with CHM. Water molecule is shown as red sphere. <scene name='91/916399/Cv/5'>Arg 49 and Arg 134</scene> (in magenra) which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shoes a movement of the <scene name='91/916399/Cv/6'>second shell residues Arg 72 and Gln 75</scene> (in lavender) which can allow the entry of the transition state analog to the active site pocket.
+==Chorismate mutase 3D structures==
+[[3D structures of chorismate mutase]]
 </StructureSection>
 == References ==
 <references/>