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090			_aB-16125
245	1	0	_aMechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
490	0		_vNature Structural Biology, 10(7), p.545-552, 2003
520	3		_aSET domain protein methyltransferases catalyze the transfer of methyl groups from the cofactor S-adenosylmethionine (AdoMet)to specific lysine residues of protein substrates, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex. The crystal structures of pea Rubisco large subunit methyltransferase (LSMT)in ternary complexes with either lysine or e-N-methyllysine (MeLys)and the product S-adenosylhomocysteine (AdoHcy)were determined to resolutions of 2.65 and 2.55 Å, respectively. The ?-methyl group of MeLys is bound to the enzyme via carbon-oxygen hydrogen bonds that play a key role in catalysis. The methyl donor and acceptor are aligned in a linear geometry for SN2 nucleophilic transfer of the methyl group during catalysis. Differences in hydrogen bonding between the MeLys e-amino group and Rubisco LSMT and SET7/9 explain why Rubisco LSMT generates multiply methylated Lys, wheras SET7/9 generates only MeLys.
650	1	4	_aEPSILON N METHYLLYSINE
650	1	4	_aHISTONE H3
650	1	4	_aHISTONE H4
650	1	4	_aHOLOENZYME
650	1	4	_aLARGE SUBUNIT METHYLTRANSFERASE
650	1	4	_aLYSINE
650	1	4	_aLYSINE DERIVATIVE
650	1	4	_aMETHYL GROUP
650	1	4	_aPROTEIN
650	1	4	_aPROTEIN METHYLTRANSFERASE
650	1	4	_aRIBULOSEBISPHOSPHATE CARBOXYLASE
650	1	4	_aS ADENOSYLHOMOCYSTEINE
650	1	4	_aS ADENOSYLMETHIONINE
650	1	4	_aSET DOMAIN PROTEIN
650	1	4	_aUNCLASSIFIED DRUG
700	1	2	_aTrievel, R.C.
700	1	2	_aFlynn, E.M.
700	1	2	_aHoutz, R.L.
700	1	2	_aHurley, J.H.
856	4	0	_uhttps://drive.google.com/file/d/1oxmsE2R9GGrqt3eOZKSvmDd8NCTq5WwM/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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