1qff: Difference between revisions

Revision as of 09:57, 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:1qff.png

Template:STRUCTURE 1qff

E. COLI FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) IN COMPLEX WITH BOUND FERRICHROME-IRONE. COLI FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) IN COMPLEX WITH BOUND FERRICHROME-IRON

Template:ABSTRACT PUBMED 10873859

About this StructureAbout this Structure

1QFF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins., Ferguson AD, Welte W, Hofmann E, Lindner B, Holst O, Coulton JW, Diederichs K, Structure. 2000 Jun 15;8(6):585-92. PMID:10873859

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OCA

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 {{STRUCTURE_1qff|  PDB=1qff  |  SCENE=  }}
-'''E. COLI FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) IN COMPLEX WITH BOUND FERRICHROME-IRON'''
+===E. COLI FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) IN COMPLEX WITH BOUND FERRICHROME-IRON===
-==Overview==
+<!--
-BACKGROUND: Lipopolysaccharide (LPS), a lipoglycan from the outer membrane of Gram-negative bacteria, is an immunomodulatory molecule that stimulates the innate immune response. High levels of LPS cause excessive release of inflammatory mediators and are responsible for the septic shock syndrome. The interaction of LPS with its cognate binding proteins has not, as yet, been structurally elucidated. RESULTS: The X-ray crystallographic structure of LPS in complex with the integral outer membrane protein FhuA from Escherichia coli K-12 is reported. It is in accord with data obtained using mass spectroscopy and nuclear magnetic resonance. Most of the important hydrogen-bonding or electrostatic interactions with LPS are provided by eight positively charged residues of FhuA. Residues in a similar three-dimensional arrangement were searched for in all structurally known proteins using a fast template-matching algorithm, and a subset of four residues was identified that is common to known LPS-binding proteins. CONCLUSIONS: These four residues, three of which form specific interactions with lipid A, appear to provide the structural basis of pattern recognition in the innate immune response. Their arrangement can serve to identify LPS-binding sites on proteins known to interact with LPS, and could serve as a template for molecular modeling of a LPS scavenger designed to reduce the septic shock syndrome.
+The line below this paragraph, {{ABSTRACT_PUBMED_10873859}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10873859 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10873859}}
 ==About this Structure==
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 [[Category: Siderophore-iron receptor]]
 [[Category: Tonb-dependent receptor]]
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