4OU7

Crystal structure of DnaT84-153-dT10 ssDNA complex reveals a novel single-stranded DNA binding mode

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C	PF17948	e4ou7C1	A: alpha arrays	X: RuvA-C	H: DnaT DNA-binding domain (From Topology)	T: DnaT DNA-binding domain	F: PF17948	ECOD (1.6)
A	PF17948	e4ou7A1	A: alpha arrays	X: RuvA-C	H: DnaT DNA-binding domain (From Topology)	T: DnaT DNA-binding domain	F: PF17948	ECOD (1.6)
B	PF17948	e4ou7B1	A: alpha arrays	X: RuvA-C	H: DnaT DNA-binding domain (From Topology)	T: DnaT DNA-binding domain	F: PF17948	ECOD (1.6)
D	PF17948	e4ou7D1	A: alpha arrays	X: RuvA-C	H: DnaT DNA-binding domain (From Topology)	T: DnaT DNA-binding domain	F: PF17948	ECOD (1.6)
E	PF17948	e4ou7E1	A: alpha arrays	X: RuvA-C	H: DnaT DNA-binding domain (From Topology)	T: DnaT DNA-binding domain	F: PF17948	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	1.10.8.1180	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
A	1.10.8.1180	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
B	1.10.8.1180	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
D	1.10.8.1180	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
E	1.10.8.1180	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E	PF17948	DnaT DNA-binding domain (DnaT)	DnaT DNA-binding domain	This domain is found in E.coli primosomal protein 1 (Pp1). PP1 domain (residues 84-153) in Swiss:P0A8J2 can bind to different types of ssDNA, which is fundamental for its physiological substrate bindings. Functional analysis indicate that both N- and ...	This domain is found in E.coli primosomal protein 1 (Pp1). PP1 domain (residues 84-153) in Swiss:P0A8J2 can bind to different types of ssDNA, which is fundamental for its physiological substrate bindings. Functional analysis indicate that both N- and C- terminals are essential to having the cooperative effect in binding ssDNA. The ssDNA bound complex displays a spiral filament assembly that is adopted by many proteins that are involved in DNA replication, such as DnaA, RecA and PriB. This domain is similar to Pfam:PF08585 except that it contains an extra loop at the N-terminus (84-99). Structural analysis indicate that this extra loop might be essential for the stabilisation of the three-helix bundle [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E	Primosomal protein 1	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding identical protein binding protein binding DNA binding organic cyclic compound binding single-stranded DNA binding nucleic acid binding	DNA-templated DNA replication DNA-templated DNA replication maintenance of fidelity primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA replication organic substance metabolic process metabolic process macromolecule metabolic process replication fork processing cellular biosynthetic process DNA replication, synthesis of primer DNA-templated DNA replication DNA-templated DNA replication maintenance of fidelity primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA replication organic substance metabolic process metabolic process macromolecule metabolic process replication fork processing cellular biosynthetic process DNA replication, synthesis of primer cellular metabolic process RNA metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process RNA biosynthetic process nucleic acid biosynthetic process biosynthetic process organic cyclic compound biosynthetic process organic substance biosynthetic process cellular process protein-containing complex organization protein trimerization cellular component organization cellular component biogenesis cellular component assembly protein homotrimerization protein complex oligomerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis DNA duplex unwinding DNA geometric change chromosome organization DNA conformation change DNA unwinding involved in DNA replication organelle organization	primosome complex protein-containing complex intracellular anatomical structure protein-DNA complex chromosome cellular anatomical entity intracellular organelle organelle intracellular non-membrane-bounded organelle replication fork replisome non-membrane-bounded organelle DnaB-DnaC-DnaT-PriA-PriC complex pre-primosome complex primosome complex protein-containing complex intracellular anatomical structure protein-DNA complex chromosome cellular anatomical entity intracellular organelle organelle intracellular non-membrane-bounded organelle replication fork replisome non-membrane-bounded organelle DnaB-DnaC-DnaT-PriA-PriC complex pre-primosome complex DnaB-DnaC-DnaT-PriA-PriB complex
F [auth S]	DNA (5'-D(PTPTPTPTPTPTPTPTPTPT)-3')	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E	IPR040480	DnaT, DNA-binding domain	Domain
A, B, C, D, E	IPR020917	Primosomal protein 1	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.