7R2W: S-adenosylmethionine synthase

Name: PDB 7R2W: Mutant S-adenosylmethionine synthetase from E.coli complexed with AMPPNP and methionine
Published: 2022-07-13
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Mutant S-adenosylmethionine synthetase from E.coli complexed with AMPPNP and methionine. Determined by X-ray diffraction at 1.6 Å resolution. Released 13 Jul 2022.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Escherichia coli
Chains: 1
Atoms: 3,117
Mol. weight: 43.42 kDa
Ligands: ANP, MG
Released: 13 Jul 2022

Explore 7R2W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7R2W contains 16 α-helices and 16 β-strands across 1 chain. 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: 16 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	1
α-helix	16-34	19
β-strand	39-47	9	2
β-strand	50-58	9	2
α-helix	65-76	12
β-strand	79-80	2	3
α-helix	81-83	3
β-strand	85-86	2	3
β-strand	91-97	7	2
α-helix	112-114	3
α-helix	115-116	2
β-strand	117	1	4
β-strand	121-128	8	5
α-helix	137-154	18
β-strand	161-174	14	1
β-strand	177-190	14	1
α-helix	196-202	7
α-helix	203-208	6
α-helix	214-216	3
β-strand	222-225	4	1
α-helix	235-237	3
β-strand	241-242	2	2
β-strand	266	1	2
α-helix	271-288	18
β-strand	294-301	8	5
β-strand	303	1	4
β-strand	310-314	5	5
α-helix	323-333	11
α-helix	338-345	8
α-helix	353-356	4
α-helix	367-369	3
α-helix	374-380	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
S-adenosylmethionine synthase	A	protein	390	Escherichia coli	P0A817 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7R2W_1 S-adenosylmethionine synthase (chains A)
MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTS
AWVDIEKITRNTVREIGYVHSDMGFDANSCAVLSAIGQQSPDINQGVDRADPLEQGAGDQ
GLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVG
IDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDC
GLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVS
YAIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGH
FGREHFPWEKTDKAQLLRDAAGLKHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	1
MG	Magnesium ion	Mg	2

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

Primary citation

Evolution of homo-oligomerization of methionine S-adenosyltransferases is replete with structure-function constrains. Kleiner, D., Shapiro Tuchman, Z., Shmulevich, F. et al. Protein Sci (2022) 31:e4352-e4352. DOI 10.1002/pro.4352 · PubMed

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

7LO2 1.89 Å, S-adenosylmethionine synthetase cocrystallized with CTP
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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