8QFS: SidH from Legionella pneumophila

Cryo-EM structure of SidH from Legionella pneumophila. Determined by electron microscopy at 2.7 Å resolution. Released 11 Oct 2023.

Method
Electron microscopy
Resolution
2.7 Å
Organism
Escherichia coli 'BL21-Gold(DE3)pLysS AG'
Chains
3
Atoms
13,294
Mol. weight
324.36 kDa
Ligands
GTP, MG
Released
11 Oct 2023

Explore 8QFS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8QFS contains 86 α-helices and 35 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: 69 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix4-107
α-helix11-166
α-helix18-3215
β-strand3918
α-helix41-455
α-helix55-595
α-helix64-8724
α-helix105-12319
α-helix127-13711
α-helix141-15212
α-helix156-1572
α-helix170-1734
α-helix190-20415
α-helix230-24314
α-helix254-26613
α-helix280-28910
α-helix290-2945
α-helix295-30915
β-strand31118
α-helix3121
α-helix318-33821
α-helix389-41022
α-helix413-42614
α-helix430-4356
α-helix440-4423
α-helix445-46521
α-helix467-47812
α-helix485-4884
α-helix492-4987
α-helix502-5076
α-helix510-54637
α-helix572-60635
α-helix622-63817
α-helix642-65413
α-helix664-6674
α-helix668-6703
α-helix671-70636
α-helix708-7092
α-helix713-7175
α-helix722-7265
α-helix730-7367
α-helix737-7426
α-helix743-7497
β-strand75019
α-helix752-7587
α-helix767-7693
α-helix780-80526
α-helix822-84322
α-helix849-85810
α-helix860-8623
β-strand863110
β-strand865110
α-helix885-89612
α-helix910-92516
α-helix935-95218
α-helix961-97717
α-helix984-101229
α-helix1020-103819
α-helix1242-125817
α-helix1277-128711
α-helix1297-131115
α-helix1328-134821
β-strand135119
α-helix13521
α-helix1355-136814
α-helix1389-140820
α-helix1412-14209
α-helix1425-143915
α-helix1501-15077
α-helix1508-15103
α-helix1517-152711
α-helix1533-155321
α-helix1561-15644
α-helix1569-158012
α-helix1583-161735
Chain C: 17 helices, 29 β-strands
ElementResiduesLengthSheet
β-strand12-1871
α-helix25-3915
α-helix47-504
α-helix54-596
β-strand66-7161
β-strand76-8161
α-helix82-832
α-helix86-883
α-helix89-968
β-strand101-10771
α-helix114-12512
β-strand131-13661
α-helix144-16017
β-strand170-17231
α-helix175-1806
α-helix183-19917
α-helix201-2033
β-strand20612
α-helix210-2112
β-strand212-21432
β-strand217-22153
β-strand225-23173
β-strand23412
β-strand237-23824
β-strand242-24652
β-strand252-25542
β-strand256-26053
β-strand265-26623
β-strand268-26924
α-helix2701
β-strand274-27963
α-helix284-2863
β-strand28915
β-strand29115
β-strand292-29432
β-strand302-311106
α-helix312-3132
α-helix314-3163
β-strand323-32427
β-strand330-33346
β-strand336-34386
α-helix344-3452
β-strand350-35127
β-strand356-367126
β-strand374-37966
β-strand382-392116

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor TuCprotein394Escherichia coli 'BL21-Gold(DE3)pLysS AG'P0CE48 (AlphaFold model)
tRNABRNA76Escherichia coli 'BL21-Gold(DE3)pLysS AG'
Protein SidHAprotein2248Escherichia coli 'BL21-Gold(DE3)pLysS AG'Q5ZRQ1
Sequence of entity 1 (C), FASTA
>8QFS_1 Elongation factor Tu (chains C)
MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARG
ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI
LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE
GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG
EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIK
PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMV
VTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS
Sequence of entity 2 (B), FASTA
>8QFS_2 tRNA (chains B)
GCCCGGAUAGCUCAGUCGGUAGAGCAGGGGAUUGAAAAUCCCCGUGXCCUUGGUUCGAUU
CCGAGUCCGGGCACCA
Sequence of entity 3 (A), FASTA
>8QFS_3 Protein SidH (chains A)
MKHHHHHHHHHHSAGLEVLFQGPMKRTIETYIIYLKEDLKIADTCKTIKDGLLKSITDKT
HFSEELATYFERDNPNAPFKVNTTDPTQVAVLKKLLNALENAEKSFRAIENIDISRDRYT
AMIAKDAVMVSYKAVHEIYAALQLINHSNSDIQDIVGPHIQKLLPQMALASKALGNFAPE
HPEESAGAVLAGVVNMLPTEKPTESESLGKLSNLIFELPHYFEELQKLIATGASGIATKS
ITSAEDYQSAMIKKANETKYYFEQLSSKSGLLAIPSYLSIVKRLIAHSTDLVNAGAPLTK
QAYLDAVAKLEDIKHNILPQLISELEMVEESMGLKPGLLTDPALEQMNKYYTQLAEQVDN
IAKAAGVLDTVSDYSDSIGGKIVRFLAGDSKKLDVGPKLTPAPDLGVLMDDVFIQKRRSN
QESRLNEARLSSEDKSVLAAANRFFDKIGSYNSIHKAWSKWSLANISQSEKDALIKEYKQ
FQPHFAALYPDIDKLVVDALTQPTGSNIVSRLYSSDYKQLWSSDHFKQVLSCKDSVLSSI
QQSLAQSEFKAKLIEKTMSHSEETAYSMNNKTTNLTTRVQPFEPLKFTLEDDKPVEYYHK
RVIAASNQILELERAQKGVAEFFNYIQKKYPHENPSFDSLDESDKEFLRKAYKTFQPQLL
ALKHDDINTRLVSSLTSSKPTDPPLRLTDLVSLKSGINDYLNEKISDLNQDKTTLLDKEE
EAREEQYAKNPLVAKGAELEKQTLFGQMSKLKLSKSVDDFFNKKFQTYLKDNLSPEVWKQ
LSSNGETLDFDKIPYLEFHKDSPEVAMYKQLINSMHYMKNGLEKLESLNDYGDPNNIYHR
TRFVMTTFNALVMNICFSKYYVMEAGNNPGLKAIVQEGLDLLKPLEGMPLIGDYLKTTEK
QEPPKQNIITAWKKQQAVVESGLSKGPKPKTDQQLISEQLGKIQEAIDNFDGDLEVSDSA
REKIKTQIGEFAKGISGLSFGPGSVKKILAALTKLETQLSNLDKESPEVTLGKLKDIHSE
LNAQFRAAAEYTEYHSGQKFGSYSNNISTIVSNFCNGLVSNLPLKQEPAPKVKAPEKPVT
PVITGTTNPHEVVFGTKHEEFNSVYQPYLLLKRITDEFRDQNNPYKPSFDELKEEAVSYY
DKIQPLLESVDPKFDKNFIAKHKESSTLLKAIDEVMSMRQRINNPESSFAKLKDLHLEGD
FEKEENKEKFRQLYKEIQPYLHKIDSTYDQTQFLEGLKTAKDFSGALQRIMNEENALQQS
TSLKDTSYLQLIAESLYQIPVKLNKLKAEPDTPEPSKEEIDANVKAFVEGLNGLSFGPGS
VKKILSTAAKLQMQLSDIGKEGRELTMGRLKEIQAEFGTILMAAADNAEFHLGLKPGTYS
RTVSERFEKFYSSLIVNLPLEKDQTGLELLIDTTSTQKRLAREMERLESVKEDTSAIDTK
KSIFGTEHEQFSTLYQPYASLRHIAKDIEDGVHMNLYERTLEELKEEASNEYKKIQPYLA
KINPEFTEDYISKTDGEYSLLHAIDRVFEERHKINKPSSPFDKLRDLYLDGDFEKEENKE
QFLQLYAELQPHLIKINYQYDLAYFLRELQTPEDFKAATERIINDESKLQELITGLDDTK
RLKVKLCEERIGYFIDLLKKQELEVGPEKIQAFKEKIFFNYIHANVNSALDAKIGSHAEQ
FLQFIEKDFLDKKNEILEKITIDQDMEEEIAKAIDRIAPDIINNKIESFKKLLFDSYIQS
DIKNSLHNELGIYTSLFIDKISPEIHLHQSEILGNVAFDSKMGAEIGSKINAITPGILLN
NNPLKEAYVDLNNTLKEINTLLDEENKKTRDNPCRNEKIAKLTSLKDRLSDLDSIPKENT
VEFLKKMQEETRSSLKSLESNDALINIYDVLNSLKETIENGSDLPEIKKDKLQMISDVQN
ILSNFDKNPAERLNLAVQILNDSNPEVLSKTKGNFLIGEAFKGQVFTNYINTKISEQLNN
ELGPYGKVFLKQIMPDFIAKKSEIIKEIAIDNMETGLETQFKIHAPAIFEKNKELKAAYE
QLNVHLKEVQSLIEAEEKKPKGNPCREEKIAALRSHQSQLMNTQRIPDHETLRFLQEQNK
SAKSFMGKLEKYDTMISVYDSLTEIREHVSNHKSLSKEIKDEKIQEISKMEDMLKTTSKE
PSIRLAEVKAHGLSDQCKNVLLKNSDNFLVSFFKTLFSKLFNIKNENETLVSSFKQRLQN
IKGPEPVATPMETPENEAPLVNANITRF

Ligands and cofactors

IDNameFormulaCopies
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P31
MGMagnesium ionMg1

Primary citation

Structural basis for the toxicity of Legionella pneumophila effector SidH. Sharma, R., Adams, M., Griffith-Jones, S. et al. Nat Commun (2023) 14:7068-7068. DOI 10.1038/s41467-023-42683-8 · PubMed

Other PDB entries of the same protein (UniProt P0CE48 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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