Database accession: MF7000209
Name: Chorismate mutase (Corynebacterium glutamicum)
PDB ID: 5hub
Experimental method: X-ray (1.06 Å)
Assembly: Homodimer
Source organism: Corynebacterium glutamicum
Primary publication of the structure:
Burschowsky D, Thorbjørnsrud HV, Heim JB, Fahrig-Kamarauskaitė JR, Würth-Roderer K, Kast P, Krengel U
Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp.
(2018) Biochemistry 57: 557-573
PMID: 29178787
Abstract:
Corynebacterium glutamicum is widely used for the industrial production of amino acids, nucleotides, and vitamins. The shikimate pathway enzymes DAHP synthase (CgDS, Cg2391) and chorismate mutase (CgCM, Cgl0853) play a key role in the biosynthesis of aromatic compounds. Here we show that CgCM requires the formation of a complex with CgDS to achieve full activity, and that both CgCM and CgDS are feedback regulated by aromatic amino acids binding to CgDS. Kinetic analysis showed that Phe and Tyr inhibit CgCM activity by inter-enzyme allostery, whereas binding of Trp to CgDS strongly activates CgCM. Mechanistic insights were gained from crystal structures of the CgCM homodimer, tetrameric CgDS, and the heterooctameric CgCM-CgDS complex, refined to 1.1, 2.5, and 2.2 Å resolution, respectively. Structural details from the allosteric binding sites reveal that DAHP synthase is recruited as the dominant regulatory platform to control the shikimate pathway, similar to the corresponding enzyme complex from Mycobacterium tuberculosis.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
chorismate mutase activity chorismate mutase activity
Biological process:
chorismate metabolic process chorismate metabolic process
salicylic acid biosynthetic process salicylic acid biosynthetic process
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, A-2
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Chorismate mutase
Source organism: Corynebacterium glutamicum
Length: 103 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMCMTNAGDNFEIRMPSGTDDPLSDAEIQKYREEINRLDREILDAVKRRTKISQTIGKTRMSSGGTRLVHTREVAIINQFREEIGEEGPALAGILLRMGRGKLG
UniProtKB AC: Q8NS29 (positions: 21-99)
Coverage: 76%
Name: Chorismate mutase
Source organism: Corynebacterium glutamicum
Length: 103 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMCMTNAGDNFEIRMPSGTDDPLSDAEIQKYREEINRLDREILDAVKRRTKISQTIGKTRMSSGGTRLVHTREVAIINQFREEIGEEGPALAGILLRMGRGKLG
UniProtKB AC: Q8NS29 (positions: 21-99)
Coverage: 76%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Chorismate mutase type II
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555).
Chain A:
N/A
Chain A-2:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
