1M5Y

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1m5ya1	All alpha proteins	Triger factor/SurA peptide-binding domain-like	Triger factor/SurA peptide-binding domain-like	Porin chaperone SurA, peptide-binding domain	Porin chaperone SurA, peptide-binding domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1m5ya2	Alpha and beta proteins (a+b)	FKBP-like	FKBP-like	FKBP immunophilin/proline isomerase	Porin chaperone SurA, PPIase domains	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1m5yb1	All alpha proteins	Triger factor/SurA peptide-binding domain-like	Triger factor/SurA peptide-binding domain-like	Porin chaperone SurA, peptide-binding domain	Porin chaperone SurA, peptide-binding domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1m5yb2	Alpha and beta proteins (a+b)	FKBP-like	FKBP-like	FKBP immunophilin/proline isomerase	Porin chaperone SurA, PPIase domains	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1m5yc1	All alpha proteins	Triger factor/SurA peptide-binding domain-like	Triger factor/SurA peptide-binding domain-like	Porin chaperone SurA, peptide-binding domain	Porin chaperone SurA, peptide-binding domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1m5yc2	Alpha and beta proteins (a+b)	FKBP-like	FKBP-like	FKBP immunophilin/proline isomerase	Porin chaperone SurA, PPIase domains	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1m5yd1	All alpha proteins	Triger factor/SurA peptide-binding domain-like	Triger factor/SurA peptide-binding domain-like	Porin chaperone SurA, peptide-binding domain	Porin chaperone SurA, peptide-binding domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1m5yd2	Alpha and beta proteins (a+b)	FKBP-like	FKBP-like	FKBP immunophilin/proline isomerase	Porin chaperone SurA, PPIase domains	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Porin chaperone SurA peptide-binding domain	8030930	4002409	SCOP2 (2022-06-29)
A	SCOP2 Family	FKBP immunophilin/proline isomerase	8023717	4001062	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Triger factor/SurA peptide-binding domain-like	8043309	3001632	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Rotamase-like	8036097	3000622	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Rotamase-like	8036097	3000622	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Triger factor/SurA peptide-binding domain-like	8043309	3001632	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Triger factor/SurA peptide-binding domain-like	8043309	3001632	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Triger factor/SurA peptide-binding domain-like	8043309	3001632	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Rotamase-like	8036097	3000622	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Triger factor/SurA peptide-binding domain-like	8043309	3001632	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Triger factor/SurA peptide-binding domain-like	8043309	3001632	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Rotamase-like	8036097	3000622	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Triger factor/SurA peptide-binding domain-like	8043309	3001632	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF09312	e1m5yA1	A: alpha arrays	X: Triger factor/SurA peptide-binding domain-like (From Homology)	H: Triger factor/SurA peptide-binding domain-like	T: Porin chaperone SurA, peptide-binding domain	F: PF09312	ECOD (1.6)
A	PF00639	e1m5yA2	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF00639	ECOD (1.6)
A	PF13616	e1m5yA3	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF13616	ECOD (1.6)
B	PF09312	e1m5yB1	A: alpha arrays	X: Triger factor/SurA peptide-binding domain-like (From Homology)	H: Triger factor/SurA peptide-binding domain-like	T: Porin chaperone SurA, peptide-binding domain	F: PF09312	ECOD (1.6)
B	PF00639	e1m5yB2	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF00639	ECOD (1.6)
B	PF13616	e1m5yB3	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF13616	ECOD (1.6)
C	PF09312	e1m5yC1	A: alpha arrays	X: Triger factor/SurA peptide-binding domain-like (From Homology)	H: Triger factor/SurA peptide-binding domain-like	T: Porin chaperone SurA, peptide-binding domain	F: PF09312	ECOD (1.6)
C	PF00639	e1m5yC2	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF00639	ECOD (1.6)
C	PF13616	e1m5yC3	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF13616	ECOD (1.6)
D	PF09312	e1m5yD1	A: alpha arrays	X: Triger factor/SurA peptide-binding domain-like (From Homology)	H: Triger factor/SurA peptide-binding domain-like	T: Porin chaperone SurA, peptide-binding domain	F: PF09312	ECOD (1.6)
D	PF00639	e1m5yD2	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF00639	ECOD (1.6)
D	PF13616	e1m5yD3	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF13616	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.4030.10	Mainly Alpha	Orthogonal Bundle	Triger factor/SurA peptide-binding fold	Porin chaperone SurA, peptide-binding domain	CATH (4.3.0)
A	3.10.50.40	Alpha Beta	Roll	Chitinase A	domain 3	CATH (4.3.0)
B	1.10.4030.10	Mainly Alpha	Orthogonal Bundle	Triger factor/SurA peptide-binding fold	Porin chaperone SurA, peptide-binding domain	CATH (4.3.0)
B	3.10.50.40	Alpha Beta	Roll	Chitinase A	domain 3	CATH (4.3.0)
C	1.10.4030.10	Mainly Alpha	Orthogonal Bundle	Triger factor/SurA peptide-binding fold	Porin chaperone SurA, peptide-binding domain	CATH (4.3.0)
C	3.10.50.40	Alpha Beta	Roll	Chitinase A	domain 3	CATH (4.3.0)
D	1.10.4030.10	Mainly Alpha	Orthogonal Bundle	Triger factor/SurA peptide-binding fold	Porin chaperone SurA, peptide-binding domain	CATH (4.3.0)
D	3.10.50.40	Alpha Beta	Roll	Chitinase A	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF09312	SurA N-terminal domain (SurA_N)	SurA N-terminal domain	This domain is found at the N-terminal of the chaperone SurA, a chaperone that assists correct folding of outer membrane proteins (OMPs) in Gram-negative bacteria [1]. This is the helical domain found at the N-terminal of SurA that, together with the ...	This domain is found at the N-terminal of the chaperone SurA, a chaperone that assists correct folding of outer membrane proteins (OMPs) in Gram-negative bacteria [1]. This is the helical domain found at the N-terminal of SurA that, together with the C-terminal, forms a core domain which contains OMP binding sites. OMP binding induces conformational changes of SurA domains that protect OMPs from misfolding and aggregation [2]. The C-terminal of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.	Domain
A, B, C, D	PF13616	PPIC-type PPIASE domain (Rotamase_3)	PPIC-type PPIASE domain	Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.	Domain
A, B, C, D	PF00639	PPIC-type PPIASE domain (Rotamase)	PPIC-type PPIASE domain	Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Survival protein surA	isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity unfolded protein binding protein binding binding peptide binding	membrane organization membrane biogenesis membrane assembly cellular component organization cellular component biogenesis cellular component assembly cellular process cellular component organization or biogenesis cell envelope organization Gram-negative-bacterium-type cell outer membrane assembly external encapsulating structure organization regulation of protein stability biological regulation regulation of biological quality membrane organization membrane biogenesis membrane assembly cellular component organization cellular component biogenesis cellular component assembly cellular process cellular component organization or biogenesis cell envelope organization Gram-negative-bacterium-type cell outer membrane assembly external encapsulating structure organization regulation of protein stability biological regulation regulation of biological quality protein stabilization maintenance of stationary phase cellular homeostasis homeostatic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process protein folding biosynthetic process organic substance biosynthetic process metabolic process protein metabolic process macromolecule metabolic process maintenance of unfolded protein chaperone-mediated protein folding	outer membrane-bounded periplasmic space cell envelope periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR046357	Peptidyl-prolyl cis-trans isomerase domain superfamily	Homologous Superfamily
A, B, C, D	IPR027304	Trigger factor/SurA domain superfamily	Homologous Superfamily
A, B, C, D	IPR023058	Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved site	Conserved Site
A, B, C, D	IPR000297	Peptidyl-prolyl cis-trans isomerase, PpiC-type	Domain
A, B, C, D	IPR023034	Peptidyl-prolyl isomerase SurA	Family
A, B, C, D	IPR015391	SurA N-terminal	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.