7LO2: S-adenosylmethionine synthase

Name: PDB 7LO2: S-adenosylmethionine synthetase cocrystallized with CTP
Published: 2021-03-31
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

S-adenosylmethionine synthetase cocrystallized with CTP. Determined by X-ray diffraction at 1.89 Å resolution. Released 31 Mar 2021.

Method: X-ray diffraction
Resolution: 1.89 Å
Organism: Escherichia coli 908573
Chains: 4
Atoms: 12,452
Mol. weight: 170.64 kDa
Ligands: POP, PO4, MG
Released: 31 Mar 2021

Explore 7LO2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7LO2 contains 63 α-helices and 66 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	1
α-helix	15-33	19
β-strand	38-46	9	2
β-strand	49-57	9	2
α-helix	64-75	12
β-strand	78-79	2	3
α-helix	80-82	3
β-strand	84-85	2	3
β-strand	90-98	9	2
α-helix	111-113	3
α-helix	114-115	2
β-strand	116	1	4
β-strand	120-127	8	5
α-helix	136-153	18
β-strand	160-173	14	1
β-strand	176-189	14	1
α-helix	195-202	8
α-helix	203-207	5
α-helix	213-215	3
β-strand	221-224	4	1
β-strand	239-241	3	2
β-strand	265	1	2
α-helix	270-287	18
β-strand	293-300	8	5
β-strand	302	1	4
β-strand	309-313	5	5
α-helix	322-332	11
α-helix	337-344	8
α-helix	352-355	4
α-helix	366-368	3
α-helix	373-380	8

Chain B: 16 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	6
α-helix	15-33	19
β-strand	38-46	9	7
β-strand	49-57	9	7
α-helix	64-75	12
β-strand	78-79	2	8
α-helix	80-82	3
β-strand	84-85	2	8
β-strand	90-98	9	7
α-helix	111-113	3
α-helix	114-115	2
β-strand	116	1	9
β-strand	120-127	8	10
α-helix	136-153	18
β-strand	160-173	14	6
β-strand	176-189	14	6
α-helix	195-202	8
α-helix	203-207	5
α-helix	208-210	3
α-helix	213-215	3
β-strand	221-224	4	6
β-strand	240-241	2	7
β-strand	265	1	7
α-helix	270-287	18
β-strand	293-300	8	10
β-strand	302	1	9
β-strand	309-313	5	10
α-helix	322-332	11
α-helix	339-344	6
α-helix	352-355	4
α-helix	366-368	3
α-helix	373-379	7

Chain C: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	11
α-helix	15-33	19
β-strand	38-46	9	2
β-strand	49-57	9	2
α-helix	64-75	12
β-strand	78-79	2	12
α-helix	80-82	3
β-strand	84-85	2	12
β-strand	90-98	9	2
α-helix	111-113	3
α-helix	114-115	2
β-strand	116	1	13
β-strand	120-127	8	14
α-helix	136-153	18
β-strand	160-173	14	11
β-strand	176-189	14	11
α-helix	195-202	8
α-helix	203-207	5
α-helix	213-215	3
β-strand	221-224	4	11
β-strand	239-241	3	2
β-strand	265	1	2
α-helix	270-287	18
β-strand	293-300	8	14
β-strand	302	1	13
β-strand	309-313	5	14
α-helix	322-332	11
α-helix	337-344	8
α-helix	352-355	4
α-helix	366-368	3
α-helix	373-379	7

Chain D: 17 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	15
α-helix	15-33	19
β-strand	38-46	9	7
β-strand	49-57	9	7
α-helix	64-75	12
β-strand	78-79	2	16
α-helix	80-82	3
β-strand	84-85	2	16
β-strand	90-98	9	7
α-helix	111-113	3
α-helix	114-115	2
β-strand	116	1	17
β-strand	120-127	8	18
α-helix	136-153	18
β-strand	160-173	14	15
β-strand	176-189	14	15
α-helix	195-202	8
α-helix	203-207	5
α-helix	208-210	3
α-helix	213-215	3
β-strand	221-224	4	15
β-strand	240-241	2	7
α-helix	246-249	4
β-strand	265	1	7
α-helix	270-287	18
β-strand	291	1	19
β-strand	293-300	8	18
β-strand	302	1	17
β-strand	309-313	5	18
β-strand	318	1	19
α-helix	322-332	11
α-helix	337-344	8
α-helix	352-355	4
α-helix	366-368	3
α-helix	373-379	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
S-adenosylmethionine synthase	A, B, C, D	protein	384	Escherichia coli 908573	P0A817 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>7LO2_1 S-adenosylmethionine synthase (chains A, B, C, D)
MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTS
AWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQ
GLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVG
IDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDC
GLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVS
YAIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGH
FGREHFPWEKTDKAQLLRDAAGLK

Ligands and cofactors

ID	Name	Formula	Copies
POP	Pyrophosphate 2-	H2 O7 P2	4
PO4	Phosphate ion	O4 P	4
MG	Magnesium ion	Mg	8

Water and common crystallization additives (PG4, K, EDO) are not listed.

Primary citation

Substrate Dynamics Contribute to Enzymatic Specificity in Human and Bacterial Methionine Adenosyltransferases. Gade, M., Tan, L.L., Damry, A.M. et al. JACS Au (2021) 1:2349-2360. DOI 10.1021/jacsau.1c00464 · PubMed

Other PDB entries of the same protein (UniProt P0A817 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7R2W 1.6 Å, Mutant S-adenosylmethionine synthetase from E.coli complexed with AMPPNP and methionine
7LOO 1.95 Å, S-adenosyl methionine transferase cocrystallized with ATP
7LL3 2.24 Å, S-adenosylmethionine synthetase co-crystallized with UppNHp
7LOZ 2.25 Å, S-adenosylmethionine synthetase
7LOW 2.39 Å, S-adenosylmethionine synthetase
1P7L 2.5 Å, S-Adenosylmethionine synthetase complexed with AMPPNP and Met.
1RG9 2.5 Å, S-Adenosylmethionine synthetase complexed with SAM and PPNP
7LNN 2.5 Å, E. coli S-adenosyl methionine transferase co-crystallized with…
1MXA 2.8 Å, S-adenosylmethionine synthetase with ppi
1MXB 2.8 Å, S-adenosylmethionine synthetase with ADP
8BB1 2.8 Å, T3 SAM lyase in complex with S-adenosylmethionine synthase
1MXC 3.0 Å, S-adenosylmethionine synthetase with 8-br-ADP

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