Protein-glutamate O-methyltransferase

protein-glutamate O-methyltransferase
Identifiers
EC number	2.1.1.80
CAS number	9055-09-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles

CheR methyltransferase, all-alpha domain
chemotaxis receptor recognition by protein methyltransferase cher
Identifiers
Symbol	CheR_N
Pfam	PF03705
InterPro	IPR022641
SCOP	1af7
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

CheR methyltransferase, SAM binding domain
chemotaxis receptor recognition by protein methyltransferase cher
Identifiers
Symbol	CheR
Pfam	PF01739
Pfam clan	CL0063
InterPro	IPR022642
SCOP	1af7
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

In enzymology, a protein-glutamate O-methyltransferase (EC 2.1.1.80) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + protein L-glutamate $\rightleftharpoons$ S-adenosyl-L-homocysteine + protein L-glutamate methyl ester

Thus, the two substrates of this enzyme are S-adenosyl methionine and protein L-glutamic acid, whereas its two products are S-adenosylhomocysteine and protein L-glutamate methyl ester.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:protein-L-glutamate O-methyltransferase. Other names in common use include methyl-accepting chemotaxis protein O-methyltransferase, S-adenosylmethionine-glutamyl methyltransferase, methyl-accepting chemotaxis protein methyltransferase II, S-adenosylmethionine:protein-carboxyl O-methyltransferase, protein methylase II, MCP methyltransferase I, MCP methyltransferase II, protein O-methyltransferase, protein(aspartate)methyltransferase, protein(carboxyl)methyltransferase, protein carboxyl-methylase, protein carboxyl-O-methyltransferase, protein carboxylmethyltransferase II, protein carboxymethylase, protein carboxymethyltransferase, and protein methyltransferase II. This enzyme participates in bacterial chemotaxis - general and bacterial chemotaxis - organism-specific.

CheR proteins are part of the chemotaxis signaling mechanism which methylates the chemotaxis receptor at specific glutamate residues. Methyl transfer from the ubiquitous S-adenosyl-L-methionine (AdoMet/SAM) to either nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalysed by methyltransferases (Mtases) and modifies DNA, RNA, proteins and small molecules, such as catechol for regulatory purposes. The various aspects of the role of DNA methylation in prokaryotic restriction-modification systems and in a number of cellular processes in eukaryotes including gene regulation and differentiation is well documented.

Flagellated bacteria swim towards favourable chemicals and away from deleterious ones. Sensing of chemoeffector gradients involves chemotaxis receptors, transmembrane (TM) proteins that detect stimuli through their periplasmic domains and transduce the signals via their cytoplasmic domains .^[1] Signalling outputs from these receptors are influenced both by the binding of the chemoeffector ligand to their periplasmic domains and by methylation of specific glutamate residues on their cytoplasmic domains. Methylation is catalysed by CheR, an S-adenosylmethionine-dependent methyltransferase,^[1] which reversibly methylates specific glutamate residues within a coiled coil region, to form gamma-glutamyl methyl ester residues.^[1][2] The structure of the Salmonella typhimurium chemotaxis receptor methyltransferase CheR, bound to S-adenosylhomocysteine, has been determined to a resolution of 2.0 Angstrom.^[1] The structure reveals CheR to be a two-domain protein, with a smaller N-terminal helical domain linked via a single polypeptide connection to a larger C-terminal alpha/beta domain. The C-terminal domain has the characteristics of a nucleotide-binding fold, with an insertion of a small anti-parallel beta-sheet subdomain. The S-adenosylhomocysteine-binding site is formed mainly by the large domain, with contributions from residues within the N-terminal domain and the linker region.^[1]

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1AF7 and 1BC5.

References

1. ^ ^{a b c d e} Djordjevic S, Stock AM (April 1997). "Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine". Structure 5 (4): 545–58. doi:10.1016/S0969-2126(97)00210-4. PMID 9115443. 
2. ^ Djordjevic S, Stock AM (June 1998). "Chemotaxis receptor recognition by protein methyltransferase CheR". Nat. Struct. Biol. 5 (6): 446–50. doi:10.1038/nsb0698-446. PMID 9628482. 

Further reading

• Burgess-Cassler A, Ullah AH, Ordal GW (1982). "Purification and characterization of Bacillus subtilis methyl-accepting chemotaxis protein methyltransferase II". J. Biol. Chem. 257 (14): 8412–7. PMID 6806296. 
• Kleene SJ, Toews ML, Adler J (1977). "Isolation of glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis". J. Biol. Chem. 252 (10): 3214–8. PMID 16888. 
• Simms SA, Stock AM, Stock JB (1987). "Purification and characterization of the S-adenosylmethionine:glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria". J. Biol. Chem. 262 (18): 8537–43. PMID 3298235. 
• Springer WR, Koshland DE Jr (1977). "Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system". Proc. Natl. Acad. Sci. U. S. A. 74 (2): 533–7. doi:10.1073/pnas.74.2.533. PMC 392324. PMID 322131. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=392324. 

This article includes text from the public domain Pfam and InterPro IPR022641

This article includes text from the public domain Pfam and InterPro IPR022642