2MOQ

Solution Structure and Molecular determinants of Hemoglobin Binding of the first NEAT Domain of IsdB in Staphylococcus aureus

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	d2moqa_	All beta proteins	Immunoglobulin-like beta-sandwich	NEAT domain-like	automated matches	automated matches	Firmicutes (Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	NEAT domain	8085272	4007541	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	NEAT domain-like	8085273	3002054	SCOP2 (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	PF05031	e2moqA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF05031	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1850	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF05031	Iron Transport-associated domain (NEAT)	Iron Transport-associated domain	NEAT domains are heme and/or hemoprotein-binding modules highly conserved in secondary structure [1]. They have roles in hemoprotein binding, heme extraction and heme transfer [2]	Domain
A	PF20861	Iron-regulated surface determinant protein H/B, linker domain (Isd_H_B_linker)	Iron-regulated surface determinant protein H/B, linker domain	The bacterial pathogen Staphylococcus aureus uses two closely related receptors located on its surface, IsdH and IsdB, to capture from haemoglobin (Hb) the iron it needs to grow. Both proteins show conserved near iron transporter (NEAT) domains (Pfam ...	The bacterial pathogen Staphylococcus aureus uses two closely related receptors located on its surface, IsdH and IsdB, to capture from haemoglobin (Hb) the iron it needs to grow. Both proteins show conserved near iron transporter (NEAT) domains (Pfam:PF05031) that function synergistically. These domains, essential for the arrest of iron, are appropriately positioned by an alpha-helical linker domain (this entry), which does not interact itself with the heme group. In IsdH, this linker domain forms a three-helix bundle structure that is essential for efficient heme capture [1-4].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Iron-regulated surface determinant protein B	heme transmembrane transporter activity transporter activity transmembrane transporter activity cation binding ion binding binding metal ion binding small molecule binding	-	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR005877	YSIRK Gram-positive signal peptide	Domain
A	IPR006635	NEAT domain	Domain
A	IPR048652	Iron-regulated surface determinant protein H/B, linker domain	Domain
A	IPR019929	Iron-regulated surface determinant protein IsdB	Family
A	IPR037250	NEAT domain superfamily	Homologous Superfamily
A	IPR019931	LPXTG cell wall anchor domain	Domain

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.