3B2E: S. cerevisiae Get3 in the open conformation

Crystal structure of S. cerevisiae Get3 in the open conformation in complex with Get1 cytosolic domain. Determined by X-ray diffraction at 3.0 Å resolution. Released 27 Jun 2012.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Saccharomyces cerevisiae
Chains: 8
Atoms: 12,146
Mol. weight: 204.06 kDa
Ligands: ADP
Released: 27 Jun 2012

Explore 3B2E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3B2E contains 82 α-helices and 40 β-strands across 8 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: 17 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	10-14	5
β-strand	20-24	5	1
α-helix	31-44	14
β-strand	51-55	5	1
α-helix	61-66	6
β-strand	75-76	2	1
β-strand	78	1	2
β-strand	80	1	2
β-strand	83-87	5	1
α-helix	90-93	4
α-helix	128-132	5
α-helix	136-155	20
β-strand	162-166	5	1
α-helix	176-178	3
α-helix	179-184	6
α-helix	219-230	12
β-strand	236-243	8	1
α-helix	246-262	17
β-strand	266-274	9	1
α-helix	277-279	3
α-helix	286-305	20
β-strand	310-315	6	1
α-helix	324-331	8
α-helix	332-334	3
α-helix	338	1
α-helix	342-347	6

Chain B: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	10-14	5
β-strand	20-24	5	3
α-helix	31-44	14
β-strand	51-55	5	3
α-helix	61-66	6
β-strand	75-76	2	3
β-strand	78	1	4
β-strand	80	1	4
β-strand	83-87	5	3
α-helix	136-155	20
β-strand	162-166	5	3
α-helix	176-178	3
α-helix	179-187	9
α-helix	199-202	4
α-helix	212-215	4
α-helix	219-222	4
α-helix	226-228	3
β-strand	236-243	8	3
α-helix	246-262	17
β-strand	266-274	9	3
α-helix	288-305	18
β-strand	310-315	6	3
α-helix	324-331	8
α-helix	332-334	3
α-helix	338	1
α-helix	342-347	6

Chain C: 20 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	10-14	5
β-strand	20-24	5	5
α-helix	31-44	14
β-strand	51-55	5	5
α-helix	61-66	6
β-strand	75-76	2	5
β-strand	78	1	6
β-strand	80	1	6
β-strand	83-87	5	5
α-helix	90-93	4
α-helix	136-155	20
β-strand	162-166	5	5
α-helix	176-178	3
α-helix	180-187	8
α-helix	189-192	4
α-helix	198-202	5
α-helix	203-204	2
α-helix	210-215	6
α-helix	219-222	4
β-strand	236-243	8	5
α-helix	246-262	17
β-strand	266-274	9	5
α-helix	277-279	3
α-helix	286-289	4
α-helix	290-305	16
β-strand	310-315	6	5
α-helix	324-331	8
α-helix	332-334	3
α-helix	338	1
α-helix	342-347	6

Chain D: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	10-14	5
β-strand	20-24	5	7
α-helix	31-44	14
β-strand	51-55	5	7
α-helix	61-66	6
β-strand	75-76	2	7
β-strand	78	1	8
β-strand	80	1	8
β-strand	83-87	5	7
α-helix	128-132	5
α-helix	136-155	20
β-strand	162-166	5	7
α-helix	176-178	3
α-helix	179-186	8
α-helix	213-230	18
α-helix	233-235	3
β-strand	236-243	8	7
α-helix	246-262	17
β-strand	266-274	9	7
α-helix	286-305	20
β-strand	310-315	6	7
α-helix	324-331	8
α-helix	332-334	3
α-helix	338	1
α-helix	342-347	6

Chains E and H: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	40-56	17
α-helix	65-78	14
α-helix	85-88	4

Chain F: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	37-41	5
α-helix	42-56	15
α-helix	65-78	14
α-helix	85-88	4

Chain G: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	32-37	6
α-helix	38-56	19
α-helix	65-78	14
α-helix	85-88	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATPase GET3	A, B, C, D	protein	362	Saccharomyces cerevisiae	Q12154 (AlphaFold model)
Golgi to ER traffic protein 1	E, F, G, H	protein	84	Saccharomyces cerevisiae	P53192 (AlphaFold model)

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

>3B2E_1 ATPase GET3 (chains A, B, C, D)
MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTDPAH
NLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSL
LQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQDEGETFDTVIFDTAPTGHTLRFLQLP
NTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVC
VCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLD
QIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKELEHHHH
HH

Sequence of entity 2 (E, F, G, H), FASTA

>3B2E_2 Golgi to ER traffic protein 1 (chains E, F, G, H)
TNKYHEKWISKFAPGNELSKKYLAKVKERHELKEFNNSISAQDNYAKWTKNNRKLDSLDK
EINNLKDEIQSENKAFQAHLHKLR

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	4

Primary citation

Get1 stabilizes an open dimer conformation of get3 ATPase by binding two distinct interfaces. Kubota, K., Yamagata, A., Sato, Y. et al. J Mol Biol (2012) 422:366-375. DOI 10.1016/j.jmb.2012.05.045 · 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
4XTR 2.05 Å, Structure of Get3 bound to the transmembrane domain of Pep12
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
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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