7RPI: Murine Dispatched 'T' conformation

Cryo-EM structure of murine Dispatched 'T' conformation. Determined by electron microscopy at 2.5 Å resolution. Released 27 Oct 2021.

Method
Electron microscopy
Resolution
2.5 Å
Organism
Mus musculus
Chains
1
Atoms
8,526
Mol. weight
167.89 kDa
Ligands
NAG, AV0, Y01
Released
27 Oct 2021

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

Secondary structure: helices and β-sheets

7RPI contains 54 α-helices and 31 β-strands across 1 chain. 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: 54 helices, 31 β-strands

ElementResiduesLengthSheet
α-helix180-1867
α-helix188-20821
α-helix211-2133
β-strand22411
α-helix228-24114
β-strand24312
β-strand24912
β-strand25013
α-helix254-2618
β-strand299-30684
α-helix315-32511
α-helix326-3305
α-helix335-3384
β-strand33915
α-helix347-3504
β-strand35114
α-helix353-3608
α-helix366-3683
α-helix371-38919
α-helix422-4254
α-helix426-4305
β-strand43114
β-strand43216
β-strand450-45674
β-strand45715
β-strand45814
α-helix461-4633
α-helix464-4707
β-strand47714
β-strand481-48774
α-helix491-50111
α-helix504-52118
α-helix524-54320
α-helix544-5485
α-helix556-5605
α-helix561-5688
α-helix571-58616
α-helix592-61928
α-helix620-6234
β-strand62611
α-helix627-64721
α-helix650-6578
α-helix658-6625
α-helix663-6653
α-helix682-70221
α-helix703-7075
α-helix708-7147
α-helix716-73520
α-helix739-7402
β-strand74117
α-helix742-7432
α-helix747-7493
β-strand75318
α-helix758-7647
α-helix766-7683
β-strand77016
α-helix771-7744
β-strand782-78983
β-strand79119
β-strand81019
α-helix819-83214
β-strand838110
α-helix850-8589
α-helix866-8683
α-helix881-89818
β-strand909-91243
β-strand918-92693
β-strand927110
β-strand928-93033
α-helix9311
α-helix935-95319
α-helix9571
β-strand964-96633
α-helix970-100132
β-strand1003111
α-helix1004-102724
β-strand103117
α-helix1036-106025
α-helix1066-109328
β-strand110018
α-helix1101-111919
α-helix1120-11245
α-helix1125-11328
β-strand1140111
α-helix1141-11422

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein dispatched homolog 1Aprotein1352Mus musculusQ3TDN0 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7RPI_1 Protein dispatched homolog 1 (chains A)
MARPFKFPRSYAALLADWPVVVLGMCTLLIVVCALVGVLVPELPDFSDPLLGFEPRGTTI
GQRLVTWNNMMRNTGYKATLANYPYKYAEEQARSHRDDRWSDDHHERERREVDWNFQKDS
FFCDVPSDGYSRVVFASAGGETLWNLPAIKSMCDVDNSRIRSHPQFSDLCQRTTAVSCCP
SWTLGNYIAILNNRSSCQKIVERDVSHTLKLLRTCAKHYQNGTLGPDCWDKAARRKDQLK
CTNVPRKCTKYNAVYQILHYLVDKDFMTPKTADYAVPALKYSMLFSPTEKGESMMNIYLD
NFENWNSSDGITTVTGIEFGIKHSLFQDYLLMDTVYPAIAIAIVLLIMCVYTKSMFITLM
TMFAIISSLIVSYFLYRVVFNFEFFPFMNLTALIILVGIGADDAFVLCDVWNYTKFDKPR
AETSEAVSVTLQHAALSMFVTSFTTAAAFYANYVSNITAIRCFGVYAGTAILVNYVLMVT
WLPAVIVLHERYLLNIFTCFRKPQPQAYDKSCWAVLCQKCRRVLFAVSEASRIFFEKVLP
CIVIKFRYLWLIWFLALTVGGAYIVCVNPKMKLPSLELSEFQVFRSSHPFERYDAEFKKL
FMFERVHHGEELHMPITVIWGVSPEDSGDPLNPKSKGELTLDSTFNIASPASQAWILHFC
QKLRNQTFFHQTEQQDFTSCFIETFKQWMENQDCDEPALYPCCSHCSFPYKQEVFELCIK
KAIMELDRSTGYHLNNKTPGPRFDINDTIRAVVLEFQSTFLFTLAYEKMQQFYKEVDSWI
SHELSSAPEGLSRGWFVSNLEFYDLQDSLSDGTLIAMGLSVAVAFSVMLLTTWNIIISLY
AIVSIAGTIFVTVGSLVLLGWELNVLESVTISVAVGLSVDFAVHYGVAYRLAPDPDREGK
VIFSLSRMGSAIAMAALTTFVAGAMMMPSTVLAYTQLGTFMMLVMCVSWAFATFFFQCLC
RCLGPQGTCGQIPFPTKLQCSPFSHTLSARPGDRGPSKTHAASAYSVDARGQKSQLEHEF
YELQPLASHSCTSSEKTTYEEPHTCSEFFNGQAKNLRMPVPAAYSSELTKSPSSEPGSAL
LQSCLEQDTVCHFSLNPRCNCRDAYTHLQYGLPEIHCQQMGDSLCHKCASTAGGFVQIQS
SVAPLKASHQAAEGLLHPAQHMLPPGMQNSRPRNFFLHSVQHFQAQENLGRTSTHSTDER
LPRTAELSPPPSDSRSTESFQRACCHPENNQRRLCKSRDPGDTEGSGGTKSKVSGLPNQT
DKEEKQVEPSLLQTDETVNSEHLNHNESNFTFSHLPGEAGCRSCPNSPQSCRSIMRSKCG
TEDCQTPNLEANVPAVPTHSDLSGESLLIKTL

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O65
AV0Lauryl Maltose Neopentyl GlycolC47 H88 O222
Y01Cholesterol hemisuccinateC31 H50 O426

Water and common crystallization additives (NA) are not listed.

Primary citation

Dispatched uses Na + flux to power release of lipid-modified Hedgehog. Wang, Q., Asarnow, D.E., Ding, K. et al. Nature (2021) 599:320-324. DOI 10.1038/s41586-021-03996-0 · PubMed

Other PDB entries of the same protein (UniProt Q3TDN0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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