5GWW: MoeN5-Sso7d fusion protein

Structure of MoeN5-Sso7d fusion protein in complex with a permethylated substrate analogue. Determined by X-ray diffraction at 2.3 Å resolution. Released 20 Sept 2017.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Streptomyces ghanaensis, Sulfolobus solfataricus
Chains: 4
Atoms: 10,096
Mol. weight: 150.76 kDa
Ligands: 7B5
Released: 20 Sept 2017

Explore 5GWW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5GWW contains 71 α-helices and 10 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: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	-3-18	22
α-helix	23-30	8
α-helix	33-42	10
α-helix	49-74	26
α-helix	81-100	20
α-helix	107-115	9
α-helix	117-129	13
α-helix	135-142	8
α-helix	143-148	6
α-helix	149-160	12
α-helix	167-192	26
α-helix	200-205	6
α-helix	211-230	20
α-helix	238-248	11
α-helix	249-253	5
α-helix	254-257	4

Chain B: 21 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	-3-18	22
α-helix	23-30	8
α-helix	33-42	10
α-helix	49-74	26
α-helix	81-100	20
α-helix	108-115	8
α-helix	117-129	13
α-helix	135-142	8
α-helix	143-148	6
α-helix	149-160	12
α-helix	167-192	26
α-helix	200-206	7
α-helix	211-230	20
α-helix	236-238	3
α-helix	239-248	10
α-helix	249-253	5
α-helix	254-257	4
α-helix	266-267	2
β-strand	268-273	6	1
β-strand	276-281	6	1
α-helix	282-284	3
β-strand	285-291	7	2
β-strand	294-300	7	2
β-strand	306-312	7	2
α-helix	313-315	3
α-helix	318-325	8

Chain C: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	-1-19	21
α-helix	23-30	8
α-helix	33-42	10
α-helix	49-74	26
α-helix	81-102	22
α-helix	106-115	10
α-helix	117-128	12
α-helix	135-142	8
α-helix	143-147	5
α-helix	148-160	13
α-helix	167-192	26
α-helix	200-205	6
α-helix	211-228	18
α-helix	238-248	11
α-helix	249-253	5
α-helix	255-257	3

Chain D: 18 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	-2-18	21
α-helix	23-30	8
α-helix	33-42	10
α-helix	49-74	26
α-helix	81-102	22
α-helix	108-115	8
α-helix	117-129	13
α-helix	135-142	8
α-helix	143-148	6
α-helix	149-160	12
α-helix	167-192	26
α-helix	200-205	6
α-helix	211-230	20
α-helix	238-247	10
α-helix	248-253	6
α-helix	255-257	3
β-strand	269-272	4	3
β-strand	277-280	4	3
β-strand	285-291	7	4
β-strand	294-301	8	4
β-strand	305-312	8	4
α-helix	313-315	3
α-helix	318-324	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MoeN5,DNA-binding protein 7d	A, B, C, D	protein	343	Streptomyces ghanaensis, Sulfolobus solfataricus	A0A010 (AlphaFold model), P39476 (AlphaFold model)

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

>5GWW_1 MoeN5,DNA-binding protein 7d (chains A, B, C, D)
MAHHHHHHVDDDDKMLAAEAANRDHVTRCVAQTGGSPDLVAHTAALRLYLRVPHFLTEWT
TDPDRRAAVSRALALDIVSMKLLDDLMDDDTGLDRVELACVCLRLHLRALHELESLARDP
KAVTDILEQDAVHLCGGQIRTKRSRATNLREWRAHASTYGSTFLGRYGALAAACGGEGQP
ADSVREFAEAFAMTITMADDLTDYDRNGERDGNLAHLMRTGAVAGQDVVDLLEELRGRAL
AAVAAPPGAPGLVPVVHLYTDDVLVRLLPRHLGEAGAGAMATVKFKYKGEEKEVDISKIK
KVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK

Ligands and cofactors

ID	Name	Formula	Copies
7B5	methyl (2R)-3-dimethoxyphosphoryloxy-2-[(2Z,6E)-3,7,11-trimethyldodeca-2,6,10-t…	C21 H37 O7 P	1

Primary citation

Complex structures of MoeN5 with substrate analogues suggest sequential catalytic mechanism. Zhang, L., Ko, T.-P., Malwal, S.R. et al. Biochem Biophys Res Commun (2019) 511:800-805. DOI 10.1016/j.bbrc.2019.02.131 · PubMed

Other PDB entries of the same protein (UniProt A0A010 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5B02 2.21 Å, Structure of the prenyltransferase MoeN5 with a fusion protein tag of Sso7d
6J8V 2.23 Å, Structure of MOEN5-SSO7D fusion protein in complex with ligand 2
5B0I 2.26 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-octyl glucoside
6J8W 2.35 Å, Structure of MOEN5-SSO7D fusion protein in complex with lig 1
5GWV 2.4 Å, Structure of MoeN5-Sso7d fusion protein in complex with a substrate analogue
5B0J 2.5 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-undecyl maltoside
5B03 2.6 Å, Structure of MoeN5-Sso7d fusion protein in complex with geranyl pyrophosphate
5B0K 2.75 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-decyl maltoside
5B0L 2.8 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-nonyl glucoside
5B00 2.95 Å, Structure of the prenyltransferase MoeN5 in complex with geranyl pyrophosphate
5B0M 3.05 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-dodecyl maltoside
5B01 3.45 Å, Structure of a prenyltransferase in its unbound form

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