3MMP: Elongation factor Tu 2, Elongation factor Ts

Structure of the Qb replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins. Determined by X-ray diffraction at 2.5 Å resolution. Released 9 Jun 2010.

Method: X-ray diffraction
Resolution: 2.5 Å
Organisms: Escherichia coli, Enterobacteria phage Qbeta
Chains: 4
Atoms: 19,419
Mol. weight: 279.84 kDa
Ligands: PXN
Released: 9 Jun 2010

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

Secondary structure: helices and β-sheets

3MMP contains 118 α-helices and 124 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: 27 helices, 38 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
α-helix	19-25	7
α-helix	33-51	19
β-strand	58-66	9	1
β-strand	69-77	9	1
α-helix	80-84	5
α-helix	86-101	16
α-helix	107-125	19
β-strand	130-138	9	1
β-strand	141-147	7	2
β-strand	151-158	8	2
α-helix	162-175	14
β-strand	179	1	3
α-helix	182-184	3
α-helix	193-201	9
α-helix	208-225	18
β-strand	227	1	3
α-helix	228-230	3
β-strand	232-233	2	4
β-strand	236-240	5	4
α-helix	241-247	7
β-strand	251-259	9	2
α-helix	271-281	11
β-strand	1011-1018	8	5
α-helix	1024-1039	16
β-strand	1067-1070	4	5
β-strand	1075-1080	6	5
α-helix	1084-1093	10
β-strand	1100-1106	7	5
α-helix	1115-1124	10
β-strand	1130-1135	6	5
α-helix	1137-1139	3
α-helix	1143-1159	17
α-helix	1164-1166	3
β-strand	1169-1171	3	5
α-helix	1174-1179	6
α-helix	1182-1198	17
α-helix	1200-1204	5
α-helix	1205-1207	3
α-helix	1209-1210	2
β-strand	1211-1213	3	6
β-strand	1216-1220	5	7
β-strand	1224-1230	7	7
β-strand	1233	1	6
β-strand	1235-1237	3	8
β-strand	1241-1246	6	6
β-strand	1248-1254	7	6
β-strand	1255-1259	5	7
β-strand	1264-1265	2	7
β-strand	1267-1269	3	8
β-strand	1273-1278	6	7
α-helix	1283-1285	3
β-strand	1288	1	9
β-strand	1290	1	9
β-strand	1291-1293	3	6
β-strand	1300-1310	11	10
α-helix	1311-1312	2
β-strand	1322	1	11
β-strand	1329-1332	4	10
β-strand	1335-1342	8	10
α-helix	1343-1344	2
β-strand	1350	1	11
β-strand	1355-1367	13	10
β-strand	1373-1378	6	10
β-strand	1381-1391	11	10

Chain C: 26 helices, 38 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
α-helix	19-25	7
α-helix	33-51	19
β-strand	58-66	9	21
β-strand	69-77	9	21
α-helix	80-84	5
α-helix	86-101	16
α-helix	107-125	19
β-strand	130-138	9	21
β-strand	141-147	7	22
β-strand	151-158	8	22
α-helix	162-175	14
β-strand	179	1	23
α-helix	182-184	3
α-helix	193-201	9
α-helix	208-225	18
β-strand	227	1	23
β-strand	232-233	2	24
β-strand	236-240	5	24
α-helix	241-247	7
β-strand	251-259	9	22
α-helix	271-281	11
β-strand	1011-1018	8	25
α-helix	1024-1039	16
β-strand	1067-1070	4	25
β-strand	1075-1080	6	25
α-helix	1084-1093	10
β-strand	1100-1106	7	25
α-helix	1115-1124	10
β-strand	1130-1135	6	25
α-helix	1137-1139	3
α-helix	1143-1159	17
α-helix	1164-1166	3
β-strand	1169-1171	3	25
α-helix	1174-1179	6
α-helix	1182-1198	17
α-helix	1200-1204	5
α-helix	1205-1207	3
α-helix	1209-1210	2
β-strand	1211-1213	3	26
β-strand	1216-1220	5	27
β-strand	1224-1230	7	27
β-strand	1233	1	26
β-strand	1235-1237	3	28
β-strand	1241-1246	6	26
β-strand	1248-1254	7	26
β-strand	1255-1259	5	27
β-strand	1264-1265	2	27
β-strand	1267-1269	3	28
β-strand	1273-1278	6	27
α-helix	1283-1285	3
β-strand	1288	1	29
β-strand	1290	1	29
β-strand	1291-1293	3	26
β-strand	1300-1310	11	30
α-helix	1311-1312	2
β-strand	1322	1	31
β-strand	1329-1332	4	30
β-strand	1335-1342	8	30
α-helix	1343-1344	2
β-strand	1350	1	31
β-strand	1355-1367	13	30
β-strand	1373-1378	6	30
β-strand	1381-1391	11	30

Chain F: 32 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	11-19	9
α-helix	29-40	12
α-helix	43-46	4
α-helix	49-53	5
α-helix	63-74	12
α-helix	88-110	23
α-helix	123-139	17
α-helix	145-151	7
α-helix	164-166	3
α-helix	169-174	6
α-helix	176	1
β-strand	177-179	3	32
α-helix	184-192	9
β-strand	200-203	4	32
β-strand	206-212	7	33
β-strand	220-224	5	33
α-helix	227-244	18
α-helix	245-247	3
α-helix	255-267	13
β-strand	270-274	5	34
β-strand	275	1	35
α-helix	278-280	3
β-strand	283	1	36
α-helix	284-290	7
α-helix	293-302	10
β-strand	306-308	3	33
β-strand	314-316	3	33
β-strand	319	1	36
α-helix	328-347	20
α-helix	351-353	3
β-strand	355-357	3	34
β-strand	360-364	5	34
α-helix	365-367	3
α-helix	368-377	10
β-strand	382	1	35
α-helix	384-386	3
β-strand	388	1	34
β-strand	393-396	4	37
β-strand	399-402	4	37
β-strand	405-406	2	37
α-helix	419-433	15
β-strand	434-435	2	38
β-strand	438-439	2	38
α-helix	440	1
α-helix	441-451	11
α-helix	456-460	5
β-strand	462-463	2	39
β-strand	472-473	2	39
α-helix	476-478	3
β-strand	483-485	3	40
β-strand	488-501	14	40
α-helix	502-504	3
α-helix	505-517	13
α-helix	536-542	7
β-strand	553-567	15	40
α-helix	569-572	4

Chain G: 33 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	11-19	9
α-helix	29-40	12
α-helix	43-46	4
α-helix	49-53	5
α-helix	63-75	13
α-helix	88-110	23
α-helix	123-139	17
α-helix	145-151	7
α-helix	164-166	3
α-helix	169-174	6
α-helix	176	1
β-strand	177-179	3	12
α-helix	181-183	3
α-helix	184-192	9
β-strand	200-203	4	12
β-strand	206-212	7	13
β-strand	220-224	5	13
α-helix	227-244	18
α-helix	245-247	3
α-helix	255-267	13
β-strand	270-274	5	14
β-strand	275	1	15
α-helix	278-280	3
β-strand	283	1	16
α-helix	284-290	7
α-helix	293-302	10
β-strand	306-308	3	13
β-strand	314-316	3	13
β-strand	319	1	16
α-helix	328-347	20
α-helix	351-353	3
β-strand	355-357	3	14
β-strand	360-364	5	14
α-helix	365-367	3
α-helix	368-377	10
β-strand	382	1	15
α-helix	384-386	3
β-strand	388	1	14
β-strand	393-396	4	17
β-strand	399-402	4	17
β-strand	405-406	2	17
α-helix	419-433	15
β-strand	434-435	2	18
β-strand	438-439	2	18
α-helix	440	1
α-helix	441-451	11
α-helix	456-460	5
β-strand	462-463	2	19
β-strand	472-473	2	19
α-helix	476-478	3
β-strand	483-485	3	20
β-strand	488-501	14	20
α-helix	502-504	3
α-helix	505-517	13
α-helix	536-542	7
β-strand	553-567	15	20
α-helix	569-572	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Elongation factor Tu 2, Elongation factor Ts	A, C	protein	678	Escherichia coli	P0A6P1 (AlphaFold model), P0CE48 (AlphaFold model)
RNA-directed RNA polymerase beta chain	F, G	protein	589	Enterobacteria phage Qbeta	P14647

Sequence of entity 1 (A, C), FASTA

>3MMP_1 Elongation factor Tu 2, Elongation factor Ts (chains A, C)
MAEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRKSGAIKAAKKAGNVAADG
VIKTKIDGNYGIILEVNCQTDFVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERV
ALVAKIGENINIRRVAALEGDVLGSYQHGARIGVLVAAKGADEELVKHIAMHVAASKPEF
IKPEDVSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSK
TVGQLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSKQSHMSKEKFERTKPHVNVG
TIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRH
YAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLN
KCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFL
DSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTC
TGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDE
GGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFA
IREGGRTVGAGVVAKVLS

Sequence of entity 2 (F, G), FASTA

>3MMP_2 RNA-directed RNA polymerase beta chain (chains F, G)
MSKTASSRNSLSAQLRRAANTRIEVEGNLALSIANDLLLAYGQSPFNSEAECISFSPRFD
GTPDDFRINYLKAEIMSKYDDFSLGIDTEAVAWEKFLAAEAECALTNARLYRPDYSEDFN
FSLGESCIHMARRKIAKLIGDVPSVEGMLRHCRFSGGATTTNNRSYGHPSFKFALPQACT
PRALKYVLALRASTHFDTRISDISPFNKAVTVPKNSKTDRCIAIEPGWNMFFQLGIGGIL
RDRLRCWGIDLNDQTINQRRAHEGSVTNNLATVDLSAASDSISLALCELLLPPGWFEVLM
DLRSPKGRLPDGSVVTYEKISSMGNGYTFELESLIFASLARSVCEILDLDSSEVTVYGDD
IILPSCAVPALREVFKYVGFTTNTKKTFSEGPFRESCGKHYYSGVDVTPFYIRHRIVSPA
DLILVLNNLYRWATIDGVWDPRAHSVYLKYRKLLPKQLQRNTIPDGYGDGALVGSVLINP
FAKNRGWIRYVPVITDHTRDRERAELGSYLYDLFSRCLSESNDGLPLRGPSGCDSADLFA
IDQLICRSNPTKISRSTGKFDIQYIACSSRVLAPYGVFQGTKVASLHEA

Ligands and cofactors

ID	Name	Formula	Copies
PXN	(2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl…	C17 H36 O8	2

Primary citation

Structure of the Qbeta replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins. Kidmose, R.T., Vasiliev, N.N., Chetverin, A.B. et al. Proc Natl Acad Sci U S A (2010) 107:10884-10889. DOI 10.1073/pnas.1003015107 · PubMed

Other PDB entries of the same protein (UniProt P0A6P1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4PC3 1.83 Å, Elongation factor Tu:Ts complex with partially bound GDP
1EFU 2.5 Å, Elongation factor complex ef-tu/ef-ts from escherichia coli
4Q7J 2.9 Å, Complex structure of viral RNA polymerase
4R71 3.21 Å, Structure of the Qbeta holoenzyme complex in the P1211 crystal form
4PC7 3.6 Å, Elongation factor Tu:Ts complex in a near GTP conformation.

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