7UTT: Cyclic GMP-AMP synthase

Structure of Non-hydrolyzable ATP (ApCpp) binds to Cyclic GMP AMP synthase (cGAS) through Mn coordination. Determined by X-ray diffraction at 2.04 Å resolution. Released 3 May 2023.

Method: X-ray diffraction
Resolution: 2.04 Å
Organisms: Mus musculus, DNA molecule
Chains: 6
Atoms: 7,601
Mol. weight: 108.7 kDa
Ligands: APC, ZN, MN
Released: 3 May 2023

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

Secondary structure: helices and β-sheets

7UTT contains 36 α-helices and 28 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: 18 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	150-157	8
α-helix	158-160	3
α-helix	161-182	22
β-strand	193-197	5	1
β-strand	211-219	9	1
β-strand	225-227	3	1
β-strand	234-237	4	1
α-helix	249-251	3
β-strand	252-253	2	2
β-strand	256-257	2	2
α-helix	259-275	17
β-strand	282-284	3	1
β-strand	293-298	6	1
β-strand	304-314	11	1
α-helix	317-319	3
α-helix	320-322	3
α-helix	334-341	8
β-strand	345-349	5	1
α-helix	359-361	3
β-strand	363-366	4	1
α-helix	368-376	9
β-strand	381	1	3
α-helix	394-411	18
α-helix	413-415	3
α-helix	420-433	14
α-helix	437-440	4
α-helix	442-444	3
α-helix	445-461	17
β-strand	466	1	4
β-strand	474	1	4
α-helix	483-498	16
α-helix	502-505	4

Chain C: 18 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	150-157	8
α-helix	159-160	2
α-helix	161-184	24
β-strand	193-197	5	5
β-strand	211-219	9	5
β-strand	224-227	4	5
β-strand	234-238	5	5
α-helix	249-251	3
β-strand	252-253	2	5
β-strand	256-257	2	5
α-helix	259-275	17
β-strand	281-284	4	5
β-strand	293-299	7	5
β-strand	303-314	12	5
α-helix	317-319	3
α-helix	320-322	3
α-helix	334-342	9
β-strand	345-348	4	5
α-helix	350-352	3
β-strand	363-366	4	5
α-helix	368-376	9
β-strand	381	1	3
α-helix	394-411	18
α-helix	413-415	3
α-helix	420-433	14
α-helix	437-440	4
α-helix	442-444	3
α-helix	445-462	18
β-strand	466	1	6
β-strand	474	1	6
α-helix	483-498	16
α-helix	502-505	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cyclic GMP-AMP synthase	A, C	protein	364	Mus musculus	Q8C6L5 (AlphaFold model)
Palindromic DNA18	E, F, I, J	DNA	18	DNA molecule

Sequence of entity 1 (A, C), FASTA

>7UTT_1 Cyclic GMP-AMP synthase (chains A, C)
GTGPDKLKKVLDKLRLKRKDISEAAETVNKVVERLLRRMQKRESEFKGVEQLNTGSYYEH
VKISAPNEFDVMFKLEVPRIELQEYYETGAFYLVKFKRIPRGNPLSHFLEGEVLSATKML
SKFRKIIKEEVKEIKDIDVSVEKEKPGSPAVTLLIRNPEEISVDIILALESKGSWPISTK
EGLPIQGWLGTKVRTNLRREPFYLVPKNAKDGNSFQGETWRLSFSHTEKYILNNHGIEKT
CCESSGAKCCRKECLKLMKYLLEQLKKEFQELDAFCSYHVKTAIFHMWTQDPQDSQWDPR
NLSSCFDKLLAFFLECLRTEKLDHYFIPKFNLFSQELIDRKSKEFLSKKIEYERNNGFPI
FDKL

Sequence of entity 2 (E, F, I, J), FASTA

>7UTT_2 Palindromic DNA18 (chains E, F, I, J)
ATCTGTACATGTACAGAT

Ligands and cofactors

ID	Name	Formula	Copies
APC	Diphosphomethylphosphonic acid adenosyl ester	C11 H18 N5 O12 P3	2
ZN	Zinc ion	Zn	2
MN	Manganese (II) ion	Mn	4

Primary citation

Structure of Non-hydrolyzable ATP (ApCpp) binds to Cyclic GMP AMP synthase (cGAS) through Mn coordination. Wu, S., Gabelli, S.B., Sohn, J.S. To be published.

Other PDB entries of the same protein (UniProt Q8C6L5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8SHK 1.71 Å, Structure of binary complex of mouse cGAS and bound ATP
8SHU 1.71 Å, Structure of mouse cGAS
8SHY 1.77 Å, Structure of binary complex of mouse cGAS QN and bound ATP
5XZG 1.83 Å, Mouse cGAS bound to the inhibitor RU521
4O6A 1.86 Å, Mouse cyclic GMP-AMP synthase (cGAS) in complex with DNA
4K98 1.94 Å, Structure of Ternary Complex of cGAS with dsDNA and Bound 5 -pppG(2 ,5 )pG
4K99 1.95 Å, Structure of Ternary Complex of cGAS with dsDNA and Bound 5 -pppdG(2 ,5 )pdG
4K8V 2.0 Å, Structure of cyclic GMP-AMP Synthase (cGAS)
4K96 2.08 Å, Structure of Binary Complex of cGAS with Bound dsDNA
5XZB 2.13 Å, Mouse cGAS bound to the inhibitor RU365
7BUJ 2.13 Å, mcGAS bound with pppGpG
5XZE 2.18 Å, Mouse cGAS bound to the inhibitor RU332

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