4GU4: T1L reovirus attachment protein sigma1

Crystal structure of the T1L reovirus attachment protein sigma1 in complex with alpha-2,3-sialyllactose. Determined by X-ray diffraction at 3.5 Å resolution. Released 5 Dec 2012.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: Mammalian orthoreovirus 1
Chains: 3
Atoms: 4,912
Mol. weight: 75.24 kDa
Released: 5 Dec 2012

Explore 4GU4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GU4 contains 14 α-helices and 60 β-strands across 3 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: 5 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	268-269	2	1
β-strand	274-278	5	2
β-strand	281-285	5	2
β-strand	288	1	3
β-strand	293-296	4	4
β-strand	299-302	4	4
α-helix	305-309	5
β-strand	310-311	2	5
β-strand	315-318	4	6
β-strand	323-326	4	6
α-helix	328-331	4
β-strand	333-345	13	7
β-strand	348-361	14	7
β-strand	364-369	6	7
α-helix	370-371	2
β-strand	372-375	4	7
β-strand	381-386	6	7
β-strand	391	1	7
α-helix	392	1
α-helix	397-400	4
β-strand	410-419	10	7
β-strand	424-437	14	7
β-strand	440-447	8	7
β-strand	455-458	4	7
β-strand	461-466	6	7

Chain B: 5 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	268-269	2	8
β-strand	273-278	6	1
β-strand	281-286	6	1
β-strand	288	1	9
β-strand	293-296	4	3
β-strand	299-302	4	3
α-helix	305-309	5
β-strand	310-311	2	10
β-strand	315-318	4	5
β-strand	323-326	4	5
α-helix	328-331	4
β-strand	333-345	13	11
β-strand	348-361	14	11
β-strand	364-369	6	11
α-helix	370-371	2
β-strand	372-375	4	11
β-strand	381-386	6	11
β-strand	391	1	11
α-helix	392	1
α-helix	397-400	4
β-strand	410-420	11	11
β-strand	423-437	15	11
β-strand	440-447	8	11
β-strand	455-458	4	11
β-strand	461-466	6	11

Chain C: 4 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	268	1	2
β-strand	273-278	6	8
β-strand	281-286	6	8
β-strand	288	1	4
β-strand	293-296	4	9
β-strand	299-302	4	9
α-helix	305-309	5
β-strand	310-311	2	6
β-strand	315-318	4	10
β-strand	323-326	4	10
α-helix	328-331	4
β-strand	333-345	13	12
β-strand	348-361	14	12
β-strand	364-369	6	12
β-strand	372-375	4	12
β-strand	381-386	6	12
β-strand	391	1	12
α-helix	392	1
α-helix	397-400	4
β-strand	410-420	11	12
β-strand	423-437	15	12
β-strand	440-447	8	12
β-strand	455-458	4	12
β-strand	461-466	6	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Outer capsid protein sigma-1	A, B, C	protein	219	Mammalian orthoreovirus 1	P04506

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

>4GU4_1 Outer capsid protein sigma-1 (chains A, B, C)
GVLNQGVTSLESAKIDSVLPPLTVREASGVRTLSFGYDTSDFTIINSVLSLRSRLTLPTY
RYPLELDTANNRVQVADRFGMRTGTWTGQLQYQHPQLSWRANVTLNLMKVDDWLVLSFSQ
MTTNSIMADGKFVINFVSGLSSGWQTGDTEPSSTIDPLSTTFAAVQFLNNGQRIDAFRIM
GVSEWTDGELEIKNYGGTYTGHTQVYWAPWTIMYPCNVR

Primary citation

The GM2 Glycan Serves as a Functional Coreceptor for Serotype 1 Reovirus. Reiss, K., Stencel, J.E., Liu, Y. et al. PLoS Pathog (2012) 8:e1003078-e1003078. DOI 10.1371/journal.ppat.1003078 · PubMed

Other PDB entries of the same protein (UniProt P04506), best resolution first:

6GAJ 1.35 Å, Crystal structure of the T1L reovirus sigma1 coiled coil tail (iodide)
6GAK 1.43 Å, Crystal structure of the T1L reovirus sigma1 coiled coil tail (chloride)
6GAO 2.1 Å, Crystal structure of the T1L reovirus sigma1 coiled coil tail and body
4XC5 2.2 Å, Crystal structure of the T1L reovirus attachment protein SIGMA1
4ODB 3.2 Å, Crystal structure of the T1L reovirus attachment protein sigma1 in complex with…
4GU3 3.6 Å, Crystal structure of the T1L reovirus attachment protein sigma1 in complex with the GM2…
5MHS 3.7 Å, T1L reovirus sigma1 complexed with 5C6 Fab fragments

Browse structure collections

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