4E7S: Myosin-VI

Myosin VI D23R I24R R569E (MD) pre-powerstroke state. Determined by X-ray diffraction at 2.25 Å resolution. Released 19 Sept 2012.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: Sus scrofa
Chains: 2
Atoms: 12,540
Mol. weight: 183.96 kDa
Ligands: ADP, MG, PO4, VO4
Released: 19 Sept 2012

Explore 4E7S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4E7S contains 93 α-helices and 63 β-strands across 2 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: 46 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	1
β-strand	15-24	10	1
β-strand	28-33	6	1
β-strand	41-44	4	1
α-helix	45-47	3
β-strand	49-50	2	1
β-strand	61	1	2
α-helix	62-64	3
α-helix	70-82	13
β-strand	87-90	4	2
β-strand	93-97	5	2
α-helix	109-115	7
α-helix	118-119	2
α-helix	127-141	15
β-strand	145-150	6	2
β-strand	152	1	3
α-helix	157-172	16
α-helix	178-184	7
α-helix	186-193	8
β-strand	194-195	2	4
β-strand	203-204	2	4
β-strand	207-214	8	2
β-strand	220-228	9	2
α-helix	233-235	3
β-strand	245	1	4
α-helix	246-254	9
α-helix	257-262	6
α-helix	268-270	3
α-helix	272-275	4
α-helix	280-281	2
β-strand	282	1	5
α-helix	293-295	3
α-helix	298-303	6
β-strand	306	1	5
α-helix	313-326	14
α-helix	331-348	18
β-strand	352-354	3	6
β-strand	362-364	3	6
α-helix	366-368	3
α-helix	369-379	11
α-helix	383-391	9
β-strand	392-394	3	7
β-strand	408-410	3	7
α-helix	411-412	2
α-helix	413-442	30
β-strand	450-456	7	2
α-helix	457-459	3
β-strand	460	1	3
β-strand	466	1	8
α-helix	468-484	17
α-helix	485-490	6
α-helix	491-498	8
α-helix	503-505	3
α-helix	512-519	8
α-helix	525-534	10
α-helix	540-550	11
β-strand	557-558	2	8
α-helix	559-563	5
β-strand	576-581	6	8
β-strand	584-589	6	8
α-helix	593-596	4
β-strand	598	1	9
α-helix	603-610	8
α-helix	615-618	4
β-strand	642	1	9
α-helix	643-659	17
β-strand	662-669	8	2
α-helix	682-691	10
α-helix	694-701	8
β-strand	707-710	4	10
α-helix	711-718	8
α-helix	719-721	3
α-helix	726-729	4
α-helix	731-741	11
α-helix	746-748	3
β-strand	749-751	3	10
β-strand	755-758	4	10
α-helix	763-770	8
α-helix	774-788	15

Chain B: 47 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	11
β-strand	15-24	10	11
β-strand	28-33	6	11
β-strand	41-44	4	11
α-helix	45-47	3
β-strand	49-50	2	11
β-strand	61	1	12
α-helix	62-64	3
α-helix	70-82	13
β-strand	87-90	4	12
β-strand	93-97	5	12
α-helix	109-115	7
α-helix	118-119	2
α-helix	127-141	15
β-strand	145-150	6	12
α-helix	157-172	16
α-helix	178-193	16
β-strand	194-195	2	13
β-strand	203-204	2	13
β-strand	207-214	8	12
β-strand	220-228	9	12
α-helix	233-235	3
β-strand	245	1	13
α-helix	246-254	9
α-helix	257-263	7
α-helix	268-270	3
α-helix	272-275	4
α-helix	280-281	2
β-strand	282	1	14
α-helix	285-288	4
α-helix	293-295	3
α-helix	298-303	6
β-strand	306	1	14
α-helix	313-327	15
α-helix	331-348	18
β-strand	352-354	3	15
β-strand	362-364	3	15
α-helix	366-368	3
α-helix	369-378	10
α-helix	383-389	7
β-strand	392	1	16
β-strand	410	1	16
α-helix	411-412	2
α-helix	413-441	29
β-strand	450-456	7	12
α-helix	457-460	4
α-helix	468-484	17
α-helix	485-490	6
α-helix	491-499	9
α-helix	503-505	3
α-helix	512-519	8
α-helix	525-534	10
α-helix	540-550	11
β-strand	557-558	2	17
α-helix	560-563	4
α-helix	566-568	3
β-strand	576-581	6	17
β-strand	584-589	6	17
α-helix	593-596	4
β-strand	598	1	18
α-helix	600-602	3
α-helix	603-610	8
α-helix	615-621	7
β-strand	642	1	18
α-helix	643-660	18
β-strand	662-669	8	12
α-helix	682-691	10
α-helix	694-701	8
β-strand	707-710	4	19
α-helix	711-719	9
α-helix	726-728	3
α-helix	731-741	11
α-helix	746-748	3
β-strand	749-751	3	19
β-strand	755-758	4	19
α-helix	763-770	8
α-helix	774-785	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin-VI	A, B	protein	798	Sus scrofa	F1RQI7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4E7S_1 Myosin-VI (chains A, B)
MDYKDDDDKGEDGKPVWAPHPTDGFQVGNIVRRGPDSLTIEPLNQKGKTFLALINQVFPA
EEDSKKDVEDNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSET
IKSYQGKSLGTMPPHVFAIADKAFRDMKVLKLSQSIIVSGESGAGKTENTKFVLRYLTES
YGTGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLE
KSRICVQGKEERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQI
LQNRKSPEYLKAGSLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNID
FEEAGSTSGGCNLKNKSTQALEYCAELLGLDQDDLRVSLTTRVMLTTAGGAKGTVIKVPL
KVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQF
CINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEARLVGILDILDE
ENRLPQPSDQHFTSAVHQKHKDHFRLSIPRKSKLAIHENIRDDEGFIIRHFAGAVCYETT
QFVEKNNDALHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSFISVGNKFKTQL
NLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASF
HELYNMYKKYMPDKLARLDPRLFCKALFKALGLNEIDYKFGLTKVFFRPGKFAEFDQIMK
SDPDHLAELVKRVNHWLI

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2
MG	Magnesium ion	Mg	2
PO4	Phosphate ion	O4 P	1
VO4	Vanadate ion	O4 V	2

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

Primary citation

Processive Steps in the Reverse Direction Require Uncoupling of the Lead Head Lever Arm of Myosin VI. Menetrey, J., Isabet, T., Ropars, V. et al. Mol Cell (2012) 48:75-86. DOI 10.1016/j.molcel.2012.07.034 · PubMed

Other PDB entries of the same protein (UniProt F1RQI7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4PFO 1.75 Å, Myosin VI motor domain in the Pi release state, space group P212121
4PJN 2.0 Å, Myosin VI motor domain in the Pi release state, space group P212121 - shortly soaked…
4PJM 2.05 Å, Myosin VI motor domain in the Pi release state, space group P212121 - soaked with PO4 -…
4PJL 2.1 Å, Myosin VI motor domain A458E mutant in the Pi release state, space group P212121 -
4E7Z 2.3 Å, Myosin VI (MD) pre-powerstroke state, P21 crystal form
4PFP 2.32 Å, Myosin VI motor domain in the Pi release state (with Pi) space group P21
4PJJ 2.4 Å, MYOSIN VI (MD-INSERT2-CAM, DELTA-INSERT1) post-rigor state - long soaking with PO4
4PK4 2.78 Å, Myosin VI motor domain in the PPS state - from a Pi release state crystal, space group…

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