7Z5C: AP-2 complex subunit alpha-2

Chimera of AP2 with FCHO2 linker domain as a fusion on Cmu2 subunit. Determined by electron microscopy at 4.16 Å resolution. Released 11 May 2022.

Method: Electron microscopy
Resolution: 4.16 Å
Organisms: Rattus norvegicus, Homo sapiens, Mus musculus
Chains: 4
Atoms: 13,707
Mol. weight: 203.37 kDa
Released: 11 May 2022

Explore 7Z5C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7Z5C contains 92 α-helices and 34 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: 40 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	12-21	10
α-helix	26-45	20
α-helix	52-67	16
α-helix	76-83	8
α-helix	88-100	13
α-helix	106-121	16
α-helix	125-138	14
α-helix	141-147	7
α-helix	151-156	6
α-helix	162-178	17
α-helix	180-182	3
α-helix	189-194	6
α-helix	195-197	3
α-helix	201-214	14
α-helix	223-237	15
β-strand	248	1	1
β-strand	253	1	1
α-helix	255-266	12
α-helix	269-271	3
α-helix	274-292	19
α-helix	294-295	2
α-helix	300-320	21
α-helix	324-338	15
α-helix	344-356	13
α-helix	363-368	6
α-helix	370-378	9
α-helix	383-396	14
α-helix	402-414	13
α-helix	421-434	14
α-helix	439-453	15
α-helix	454-456	3
α-helix	459-471	13
α-helix	476-487	12
α-helix	494-507	14
α-helix	515-517	3
α-helix	519-530	12
α-helix	535-551	17
α-helix	553-562	10
α-helix	566-569	4
α-helix	574-588	15
α-helix	592-598	7
α-helix	603-606	4

Chain B: 38 helices, 0 β-strands

Element	Residues	Length
α-helix	14-22	9
α-helix	27-42	16
α-helix	48-50	3
α-helix	51-55	5
α-helix	63-79	17
α-helix	81-85	5
α-helix	88-91	4
α-helix	101-112	12
α-helix	118-130	13
α-helix	135-150	16
α-helix	158-167	10
α-helix	174-187	14
α-helix	200-211	12
α-helix	216-226	11
α-helix	234-244	11
α-helix	254-265	12
α-helix	277-283	7
α-helix	285-290	6
α-helix	291-293	3
α-helix	296-312	17
α-helix	325-327	3
α-helix	332-344	13
α-helix	351-360	10
α-helix	361-363	3
α-helix	367-383	17
α-helix	385-387	3
α-helix	388-400	13
α-helix	404-420	17
α-helix	426-432	7
α-helix	442-453	12
α-helix	456-458	3
α-helix	462-471	10
α-helix	478-494	17
α-helix	500-507	8
α-helix	517-532	16
α-helix	534-541	8
α-helix	557-565	9
α-helix	570-574	5

Chain M: 9 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	2
β-strand	14-19	6	2
α-helix	26-32	7
α-helix	33-37	5
β-strand	47-49	3	2
β-strand	54-60	7	2
β-strand	63-69	7	2
α-helix	75-93	19
α-helix	98-103	6
α-helix	105-114	10
β-strand	116-117	2	3
β-strand	120-121	2	3
α-helix	129-132	4
β-strand	172-185	14	4
β-strand	191-205	15	4
β-strand	211-216	6	5
β-strand	245-248	4	4
β-strand	253-254	2	5
β-strand	263-265	3	5
α-helix	267-268	2
β-strand	270-279	10	4
β-strand	287-294	8	6
β-strand	300-309	10	6
β-strand	317-325	9	4
β-strand	330-337	8	6
β-strand	341-345	5	4
β-strand	350-358	9	4
β-strand	363-372	10	6
α-helix	380-382	3
α-helix	384-385	2
β-strand	386-392	7	4
β-strand	401-407	7	5
β-strand	414	1	5
β-strand	419-433	15	4

Chain S: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	7
β-strand	16-19	4	7
α-helix	25-41	17
β-strand	49-52	4	7
β-strand	55-62	8	7
β-strand	65-71	7	7
α-helix	77-94	18
α-helix	102-105	4
α-helix	107-117	11
β-strand	118-119	2	8
β-strand	122-123	2	8
α-helix	128-140	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
AP-2 complex subunit alpha-2	A	protein	621	Rattus norvegicus	P18484 (AlphaFold model)
AP-2 complex subunit beta	B	protein	591	Homo sapiens	P63010 (AlphaFold model)
AP-2 complex subunit mu	M	protein	435	Rattus norvegicus	P84092 (AlphaFold model)
AP-2 complex subunit sigma	S	protein	142	Mus musculus	P62743 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7Z5C_1 AP-2 complex subunit alpha-2 (chains A)
MPAVSKGEGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVC
KLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDL
ASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSP
DLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSA
STDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSKKV
QHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSE
FSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSI
REEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAA
KTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRAL
LLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLE
EMPPFPERESSILAKLKKKKG

Sequence of entity 2 (B), FASTA

>7Z5C_2 AP-2 complex subunit beta (chains B)
MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQT
DNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITE
YLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANA
VAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSI
CERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQY
VALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKE
YATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRK
YPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQV
QLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEV
VLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRK

Sequence of entity 3 (M), FASTA

>7Z5C_3 AP-2 complex subunit mu (chains M)
MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKR
SNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGY
PQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLES
VNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQS
IAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTK
LEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAG
MKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIK
WVRYIGRSGIYETRC

Sequence of entity 4 (S), FASTA

>7Z5C_4 AP-2 complex subunit sigma (chains S)
MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYR
RYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLA
GEIRETSQTKVLKQLLMLQSLE

Primary citation

FCHO controls AP2's initiating role in endocytosis through a PtdIns(4,5)P 2 -dependent switch. Zaccai, N.R., Kadlecova, Z., Dickson, V.K. et al. Sci Adv (2022) 8:eabn2018-eabn2018. DOI 10.1126/sciadv.abn2018 · PubMed

Other PDB entries of the same protein (UniProt P18484 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6QH5 2.56 Å, AP2 clathrin adaptor mu2T156-phosphorylated core in closed conformation
2VGL 2.6 Å, AP2 clathrin adaptor core
4UQI 2.79 Å, AP2 controls clathrin polymerization with a membrane-activated switch
7OHO 2.88 Å, Crystal structure of AP2 FCHO2 chimera
4NEE 2.88 Å, crystal structure of AP-2 alpha/simga2 complex bound to HIV-1 Nef
6URI 3.0 Å, HIV-1 Nef in complex with the CD4 cytoplasmic domain and the AP2 clathrin adaptor complex
2XA7 3.1 Å, AP2 clathrin adaptor core in active complex with cargo peptides
7OG1 3.25 Å, AP2 clathrin adaptor core in complex with cargo peptide and FCHO2
6QH7 3.4 Å, AP2 clathrin adaptor mu2T156-phosphorylated core with two cargo peptides in open+…
6OWT 3.8 Å, Structure of SIVsmm Nef and SMM tetherin bound to the clathrin adaptor AP-2 complex
6YAE 3.9 Å, AP2 core in physiological buffer
6QH6 5.0 Å, AP2 clathrin adaptor core with two cargo peptides in open+ conformation

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