7L4L: 3-oxoacyl-[acyl-carrier-protein] synthase 2

Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and C8-crypto Acyl Carrier Protein, AcpP. Determined by X-ray diffraction at 2.65 Å resolution. Released 22 Sept 2021.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Escherichia coli (strain K12)
Chains: 4
Atoms: 7,265
Mol. weight: 104.45 kDa
Ligands: DYF
Released: 22 Sept 2021

Explore 7L4L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7L4L contains 54 α-helices and 57 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: 23 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	5-13	9	1
β-strand	14	1	2
β-strand	17	1	2
α-helix	20-28	9
β-strand	34-36	3	3
β-strand	49-51	3	3
α-helix	52-54	3
α-helix	64-67	4
α-helix	72-88	17
α-helix	97-99	3
β-strand	100-105	6	1
α-helix	111-124	14
α-helix	126-128	3
α-helix	133-137	5
α-helix	141-149	9
β-strand	156-157	2	1
β-strand	159	1	4
α-helix	162-164	3
α-helix	165-179	15
β-strand	184-191	8	1
α-helix	196-204	9
β-strand	208	1	5
α-helix	215-217	3
β-strand	223	1	6
β-strand	229	1	5
β-strand	231	1	7
β-strand	232	1	3
β-strand	234-242	9	1
α-helix	243-249	7
β-strand	255-264	10	1
α-helix	277-290	14
α-helix	294-296	3
β-strand	299-301	3	1
α-helix	308-322	15
α-helix	323-327	5
β-strand	330-332	3	1
α-helix	335-338	4
β-strand	340	1	7
α-helix	342-344	3
α-helix	345-359	15
β-strand	361-362	2	8
β-strand	365	1	9
β-strand	371	1	6
α-helix	372	1
β-strand	378	1	1
β-strand	381	1	9
β-strand	385-386	2	8
β-strand	392-398	7	1
α-helix	400-402	3
β-strand	403-411	9	1

Chain B: 23 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	5-13	9	10
β-strand	14	1	11
β-strand	17	1	11
α-helix	20-28	9
β-strand	34-36	3	12
β-strand	49-51	3	12
α-helix	52-54	3
α-helix	64-67	4
α-helix	72-88	17
α-helix	97-99	3
β-strand	100-105	6	10
α-helix	111-124	14
α-helix	126-128	3
α-helix	133-137	5
α-helix	141-150	10
β-strand	156-157	2	10
β-strand	159	1	4
α-helix	162-164	3
α-helix	165-179	15
β-strand	184-191	8	10
α-helix	196-204	9
β-strand	208	1	13
α-helix	215-217	3
β-strand	223	1	14
β-strand	229	1	13
β-strand	231	1	15
β-strand	232	1	12
β-strand	234-242	9	10
α-helix	243-248	6
β-strand	255-264	10	10
α-helix	277-290	14
α-helix	294-296	3
β-strand	299-301	3	10
α-helix	308-322	15
α-helix	323-326	4
β-strand	330-332	3	10
α-helix	335-338	4
β-strand	340	1	15
α-helix	342-344	3
α-helix	345-359	15
β-strand	361-362	2	16
β-strand	365	1	17
β-strand	371	1	14
α-helix	372	1
β-strand	381	1	17
β-strand	385-386	2	16
β-strand	392-398	7	10
α-helix	400-402	3
β-strand	403-411	9	10

Chain C: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
β-strand	27	1	18
α-helix	36-50	15
α-helix	56-60	5
β-strand	64	1	18
α-helix	65-74	10

Chain D: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
β-strand	27	1	19
α-helix	36-50	15
α-helix	56-59	4
β-strand	64	1	19
α-helix	65-74	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
3-oxoacyl-[acyl-carrier-protein] synthase 2	A, B	protein	413	Escherichia coli (strain K12)	P0AAI5 (AlphaFold model)
Acyl carrier protein	C, D	protein	78	Escherichia coli (strain K12)	P0A6A8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7L4L_1 3-oxoacyl-[acyl-carrier-protein] synthase 2 (chains A, B)
MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCE
DIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHT
SLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAY
GDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLV
LEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGY
VNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRD
QAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI

Sequence of entity 2 (C, D), FASTA

>7L4L_2 Acyl carrier protein (chains C, D)
MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEA
EKITTVQAAIDYINGHQA

Ligands and cofactors

ID	Name	Formula	Copies
DYF	[(3~{R})-2,2-dimethyl-4-[[3-[2-[[(~{E})-oct-2-enoyl]amino]ethylamino]-3-oxidany…	C19 H36 N3 O8 P	2

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

Primary citation

Structure and Mechanistic Analyses of the Gating Mechanism of Elongating Ketosynthases. Mindrebo, J.T., Chen, A., Kim, W.E. et al. ACS Catal (2021) 11:6787-6799. DOI 10.1021/acscatal.1c00745

Other PDB entries of the same protein (UniProt P0AAI5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3HO9 1.9 Å, Structure of E.coli FabF(C163A) in complex with Platencin A1
3I8P 1.9 Å, Crystal structure of E. coli FabF(C163A) in complex with Platensimycin A1
3G11 2.0 Å, Structure of E. coli FabF(C163Q) in complex with dihydrophenyl platensimycin
3HO2 2.0 Å, Structure of E.coli FabF(C163A) in complex with Platencin
7L4E 2.0 Å, Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and…
2GFV 2.29 Å, Structure of E. coli FabF (KASII) C163Q mutant
6OKG 2.3 Å, Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and…
6OLT 2.35 Å, Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and…
1KAS 2.4 Å, Beta-ketoacyl-ACP synthase II from escherichia coli
2GFW 2.4 Å, Structure of wild type E. coli FabF (KASII)
2GFX 2.59 Å, Structure of E. coli FabF(C163Q) in complex with Platensimycin
3G0Y 2.6 Å, Structure of E. coli FabF(C163Q) in complex with dihydroplatensimycin

Browse structure collections

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