1si0: Difference between revisions

Revision as of 16:01, 21 February 2008

Crystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in a closed conformation

OverviewOverview

We have determined the 1.35- and 1.45-A structures, respectively, of closed and open iron-loaded forms of Mannheimia haemolytica ferric ion-binding protein A. M. haemolytica is the causative agent in the economically important and fatal disease of cattle termed shipping fever. The periplasmic iron-binding protein of this gram-negative bacterium, which has homologous counterparts in many other pathogenic species, performs a key role in iron acquisition from mammalian host serum iron transport proteins and is essential for the survival of the pathogen within the host. The ferric (Fe(3+)) ion in the closed structure is bound by a novel asymmetric constellation of four ligands, including a synergistic carbonate anion. The open structure is ligated by three tyrosyl residues and a dynamically disordered solvent-exposed anion. Our results clearly implicate the synergistic anion as the primary mediator of global protein conformation and provide detailed insights into the molecular mechanisms of iron binding and release in the periplasm.

About this StructureAbout this Structure

1SI0 is a Single protein structure of sequence from Mannheimia haemolytica with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens., Shouldice SR, Skene RJ, Dougan DR, Snell G, McRee DE, Schryvers AB, Tari LW, J Bacteriol. 2004 Jun;186(12):3903-10. PMID:15175304

Page seeded by OCA on Thu Feb 21 15:01:42 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1si0.jpg|left|200px]]<br /><applet load="1si0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1si0.jpg|left|200px]]<br /><applet load="1si0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1si0, resolution 1.35&Aring;" />
 '''Crystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in a closed conformation'''<br />
 ==Overview==
-We have determined the 1.35- and 1.45-A structures, respectively, of, closed and open iron-loaded forms of Mannheimia haemolytica ferric, ion-binding protein A. M. haemolytica is the causative agent in the, economically important and fatal disease of cattle termed shipping fever., The periplasmic iron-binding protein of this gram-negative bacterium, which has homologous counterparts in many other pathogenic species, performs a key role in iron acquisition from mammalian host serum iron, transport proteins and is essential for the survival of the pathogen, within the host. The ferric (Fe(3+)) ion in the closed structure is bound, by a novel asymmetric constellation of four ligands, including a, synergistic carbonate anion. The open structure is ligated by three, tyrosyl residues and a dynamically disordered solvent-exposed anion. Our, results clearly implicate the synergistic anion as the primary mediator of, global protein conformation and provide detailed insights into the, molecular mechanisms of iron binding and release in the periplasm.
+We have determined the 1.35- and 1.45-A structures, respectively, of closed and open iron-loaded forms of Mannheimia haemolytica ferric ion-binding protein A. M. haemolytica is the causative agent in the economically important and fatal disease of cattle termed shipping fever. The periplasmic iron-binding protein of this gram-negative bacterium, which has homologous counterparts in many other pathogenic species, performs a key role in iron acquisition from mammalian host serum iron transport proteins and is essential for the survival of the pathogen within the host. The ferric (Fe(3+)) ion in the closed structure is bound by a novel asymmetric constellation of four ligands, including a synergistic carbonate anion. The open structure is ligated by three tyrosyl residues and a dynamically disordered solvent-exposed anion. Our results clearly implicate the synergistic anion as the primary mediator of global protein conformation and provide detailed insights into the molecular mechanisms of iron binding and release in the periplasm.
 ==About this Structure==
-SI0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mannheimia_haemolytica Mannheimia haemolytica] with FE, CO3 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SI0 OCA].
+SI0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mannheimia_haemolytica Mannheimia haemolytica] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=CO3:'>CO3</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SI0 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mannheimia haemolytica]]
 [[Category: Single protein]]
-[[Category: Dougan, D.R.]]
+[[Category: Dougan, D R.]]
-[[Category: McRee, D.E.]]
+[[Category: McRee, D E.]]
-[[Category: Schryvers, A.B.]]
+[[Category: Schryvers, A B.]]
-[[Category: Shouldice, S.R.]]
+[[Category: Shouldice, S R.]]
-[[Category: Skene, R.J.]]
+[[Category: Skene, R J.]]
 [[Category: Snell, G.]]
-[[Category: Tari, L.W.]]
+[[Category: Tari, L W.]]
 [[Category: CO3]]
 [[Category: EDO]]
@@ Line 25: / Line 25: @@
 [[Category: metal binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:32:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:42 2008''