1si1: Difference between revisions

Revision as of 04:18, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1si1.png

Template:STRUCTURE 1si1

Crystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in an open conformationCrystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in an open conformation

Template:ABSTRACT PUBMED 15175304

About this StructureAbout this Structure

1SI1 is a Single protein structure of sequence from Mannheimia haemolytica. 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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in an open conformation'''
+===Crystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in an open conformation===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15175304}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Tari, L W.]]
 [[Category: Metal binding protein]]
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