PDBsum entry 1qw0

Metal binding protein

PDB id

1qw0

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Contents

			Protein chain

					308 a.a. *

			Ligands

					PO4

			Metals

					_FE ×4

			Waters ×196

* Residue conservation analysis

PDB id:

1qw0

Links

Name:

Metal binding protein

Title:

Crystal structure of haemophilus influenzae n175l mutant holo ferric ion-binding protein a

Structure:

Iron-utilization periplasmic protein. Chain: a. Synonym: major ferric iron binding protein, iron-regulated 40 kda protein, mirp, fe(3+)- binding protein. Engineered: yes. Mutation: yes

Source:

Haemophilus influenzae. Organism_taxid: 727. Gene: fbpa. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.90Å

R-factor:

0.222

R-free:

0.271

Authors:

S.R.Shouldice,R.J.Skene,D.R.Dougan,D.E.Mcree,L.W.Tari,A.B.Schryvers

Key ref:

S.R.Shouldice et al. (2003). Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A. Biochemistry, 42, 11908-11914. PubMed id: 14556621 DOI: 10.1021/bi035389s

Date:

29-Aug-03

Release date:

04-Nov-03

PROCHECK

	Headers

	References

Protein chain

P35755 (FBPA_HAEIN) - Iron-utilization periplasmic protein from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Seq: Struc:					332 a.a. 308 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1021/bi035389s	Biochemistry 42:11908-11914 (2003)
PubMed id: 14556621

Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A.
S.R.Shouldice, R.J.Skene, D.R.Dougan, D.E.McRee, L.W.Tari, A.B.Schryvers.

ABSTRACT

The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. In this study, we report the crystal structures of two mutant forms of ferric ion-binding protein A (FbpA) from Haemophilus influenzae with bound multinuclear oxo-metal clusters. Crystals of site-directed mutants in the metal or anion binding ligands contain protein in the open conformation, and two mutant FbpAs, H9A and N175L, contain different cluster arrangements in the iron-binding pocket. The iron clusters are anchored by binding to the two tyrosine ligands (Tyr195 and Tyr196) positioned at the vertex of the iron-binding pocket but are not coordinated by the other metal binding ligands. Our results suggest that the metal clusters may have formed in situ, suggesting that the mutant FbpAs may serve as a simple model for protein-mediated mineralization.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20799927

H.K.Khambati, T.F.Moraes, J.Singh, S.R.Shouldice, R.H.Yu, and A.B.Schryvers (2010).
The role of vicinal tyrosine residues in the function of Haemophilus influenzae ferric-binding protein A.

Biochem J, 432, 57-64.

PDB codes:

3kn7 3kn8 3od7 3odb

17121816

N.M.Koropatkin, D.W.Koppenaal, H.B.Pakrasi, and T.J.Smith (2007).
The structure of a cyanobacterial bicarbonate transport protein, CmpA.

J Biol Chem, 282, 2606-2614.

PDB codes:

2i48 2i49 2i4b 2i4c

15342592

D.S.Anderson, P.Adhikari, A.J.Nowalk, C.Y.Chen, and T.A.Mietzner (2004).
The hFbpABC transporter from Haemophilus influenzae functions as a binding-protein-dependent ABC transporter with high specificity and affinity for ferric iron.

J Bacteriol, 186, 6220-6229.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.