4XTR: Get3

Structure of Get3 bound to the transmembrane domain of Pep12. Determined by X-ray diffraction at 2.05 Å resolution. Released 18 Mar 2015.

Method: X-ray diffraction
Resolution: 2.05 Å
Organisms: Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiens, synthetic construct
Chains: 7
Atoms: 12,729
Mol. weight: 181.81 kDa
Ligands: ADP, MG, ZN, ATP
Released: 18 Mar 2015

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

Secondary structure: helices and β-sheets

4XTR contains 68 α-helices and 102 β-strands across 7 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: 15 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
β-strand	20-25	6	1
α-helix	31-45	15
β-strand	51-55	5	1
α-helix	62-66	5
β-strand	75-76	2	1
α-helix	77	1
β-strand	83-87	5	1
α-helix	90-99	10
α-helix	125-130	6
α-helix	136-153	18
β-strand	162-166	5	1
α-helix	167-169	3
α-helix	170-177	8
α-helix	179-193	15
α-helix	212-230	19
β-strand	236-243	8	1
α-helix	246-261	16
β-strand	268-274	7	1
α-helix	286-305	20
β-strand	310-315	6	1
α-helix	324-335	12
α-helix	343-348	6

Chain B: 16 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
β-strand	20-25	6	2
α-helix	31-45	15
β-strand	51-55	5	2
α-helix	62-66	5
β-strand	75-76	2	2
α-helix	77	1
β-strand	83-86	4	2
α-helix	90-102	13
α-helix	126-130	5
α-helix	136-154	19
β-strand	162-166	5	2
α-helix	167-169	3
α-helix	170-177	8
α-helix	179-194	16
α-helix	212-230	19
β-strand	236-243	8	2
α-helix	246-261	16
β-strand	268-274	7	2
α-helix	286-305	20
β-strand	310-315	6	2
α-helix	316-317	2
α-helix	324-335	12
α-helix	344-348	5

Chain C: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	3
β-strand	14-15	2	4
β-strand	21-28	8	3
α-helix	32-34	3
β-strand	35-42	8	5
β-strand	48-55	8	5
β-strand	60-63	4	5
β-strand	71-76	6	3
β-strand	81-86	6	3
α-helix	91-93	3
β-strand	95-103	9	5
β-strand	106-112	7	5
β-strand	116-118	3	5
β-strand	119-120	2	4
α-helix	123-125	3
β-strand	126	1	6
α-helix	127-128	2
β-strand	129-133	5	7
α-helix	134-136	3
β-strand	144-154	11	7
β-strand	155	1	6
β-strand	160-163	4	8
α-helix	164-166	3
β-strand	172-174	3	7
α-helix	175-177	3
β-strand	178-179	2	7
β-strand	185-194	10	7
α-helix	197-200	4
β-strand	204-209	6	8
α-helix	210-212	3
β-strand	214-219	6	8

Chain D: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	9
β-strand	11-14	4	10
β-strand	20-26	7	9
β-strand	34-39	6	10
β-strand	46-50	5	10
β-strand	54-55	2	10
α-helix	56	1
β-strand	63-68	6	9
β-strand	71-76	6	9
α-helix	81-83	3
β-strand	86-91	6	10
β-strand	100-101	2	10
β-strand	105-109	5	10
β-strand	114	1	11
α-helix	115-116	2
β-strand	117-121	5	12
α-helix	122-124	3
α-helix	125-130	6
β-strand	132-142	11	12
β-strand	143	1	11
β-strand	148-153	6	13
β-strand	156-157	2	13
β-strand	162-166	5	12
α-helix	167-170	4
β-strand	176-185	10	12
α-helix	186-189	4
β-strand	194-200	7	13
β-strand	208-213	6	13

Chain E: 12 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	14
β-strand	13-15	3	15
β-strand	21-28	8	14
α-helix	32-34	3
β-strand	35-42	8	15
β-strand	48-55	8	15
α-helix	56-58	3
β-strand	60-63	4	15
β-strand	71-76	6	14
β-strand	81-86	6	14
α-helix	91-93	3
β-strand	95-103	9	15
β-strand	106-112	7	15
β-strand	116-120	5	15
α-helix	123-125	3
β-strand	126	1	16
α-helix	127-128	2
β-strand	129-133	5	17
α-helix	134-136	3
α-helix	139-140	2
β-strand	144-154	11	17
β-strand	155	1	16
β-strand	160-163	4	18
α-helix	164-166	3
β-strand	168	1	18
β-strand	172-174	3	17
α-helix	175-177	3
β-strand	178-179	2	17
β-strand	185-194	10	17
α-helix	195-197	3
β-strand	204-209	6	18
α-helix	210-212	3
β-strand	214-219	6	18
α-helix	222-224	3

Chain F: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	19
β-strand	11-14	4	20
β-strand	20-26	7	19
β-strand	34-39	6	20
β-strand	46-50	5	20
β-strand	54-55	2	20
α-helix	56	1
β-strand	63-68	6	19
β-strand	71-76	6	19
α-helix	81-83	3
β-strand	86-91	6	20
β-strand	100-101	2	20
β-strand	105-109	5	20
β-strand	114	1	21
α-helix	115-116	2
β-strand	117-121	5	22
α-helix	122-124	3
α-helix	125-128	4
β-strand	132-142	11	22
β-strand	143	1	21
β-strand	148-153	6	23
β-strand	156-157	2	23
α-helix	158	1
β-strand	162-166	5	22
α-helix	167-170	4
β-strand	176-185	10	22
α-helix	186-191	6
β-strand	194-200	7	23
β-strand	208-213	6	23

Chain G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	267-285	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATPase GET3	A, B	protein	354	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	Q12154 (AlphaFold model)
Antibody Heavy chain	C, E	protein	230	Homo sapiens, synthetic construct	P01857 (AlphaFold model)
Antibody Light chain	D, F	protein	217	Homo sapiens, synthetic construct	P01834 (AlphaFold model)
Pep12p	G	protein	37	Saccharomyces cerevisiae	P32854 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4XTR_1 ATPase GET3 (chains A, B)
MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTNPAH
NLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSL
LQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQGEGETFDTVIFDTAPTGHTLRFLQLP
NTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVC
VCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLD
QIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKE

Sequence of entity 2 (C, E), FASTA

>4XTR_2 Antibody Heavy chain (chains C, E)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNLYYYSIHWVRQAPGKGLEWVASISPYSSS
TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARGRWYRRALDYWGQGTLVTV
SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Sequence of entity 3 (D, F), FASTA

>4XTR_3 Antibody Light chain (chains D, F)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYPYYSSLITFGQGTKVEIKRTVAAPSVFI
FPPSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSS
TLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 4 (G), FASTA

>4XTR_4 Pep12p (chains G)
MGSHHHHHHSKRTSRWRVYLLIVLLVMLLFIFLIMKL

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2
MG	Magnesium ion	Mg	2
ZN	Zinc ion	Zn	1
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

Primary citation

Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo. Mateja, A., Paduch, M., Chang, H.Y. et al. Science (2015) 347:1152-1155. DOI 10.1126/science.1261671 · PubMed

Other PDB entries of the same protein (UniProt Q12154 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2WOJ 1.99 Å, ADP-AlF4 complex of S. cerevisiae GET3
3ZS9 2.1 Å, S. cerevisiae Get3-ADP-AlF4- complex with a cytosolic Get2 fragment
3H84 2.3 Å, Crystal structure of GET3
4XVU 2.35 Å, Structure of Get3 bound to the transmembrane domain of Nyv1
4XWO 2.75 Å, Structure of Get3 bound to the transmembrane domain of Sec22
3A36 2.8 Å, Structural insight into the membrane insertion of tail-anchored proteins by Get3
5BW8 2.8 Å, 2.8 A crystal structure of a Get3-Get4-Get5 intermediate complex from S.cerevisiae
3A37 3.0 Å, Structural insight into the membrane insertion of tail-anchored proteins by Get3
3B2E 3.0 Å, Crystal structure of S. cerevisiae Get3 in the open conformation in complex with Get1…
3SJA 3.0 Å, Crystal structure of S. cerevisiae Get3 in the open state in complex with Get1 cytosolic…
3ZS8 3.0 Å, S. cerevisiae Get3 complexed with a cytosolic Get1 fragment
9NS5 3.19 Å, Get3(D57N)-Get4/5 Complex (ATP-bound)

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