1qff: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1qff.jpg|left|200px]] | [[Image:1qff.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1qff", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
| | {{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''' | ||
| Line 30: | Line 27: | ||
[[Category: Hofmann, E.]] | [[Category: Hofmann, E.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
[[Category: | [[Category: Active transport]] | ||
[[Category: | [[Category: Ferrichrome receptor]] | ||
[[Category: | [[Category: Integral outer membrane protein]] | ||
[[Category: | [[Category: Lipopolysaccharide]] | ||
[[Category: | [[Category: Siderophore-iron receptor]] | ||
[[Category: | [[Category: Tonb-dependent receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:12:13 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 06:12, 3 May 2008
E. COLI FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) IN COMPLEX WITH BOUND FERRICHROME-IRON
OverviewOverview
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.
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 Page seeded by OCA on Sat May 3 06:12:13 2008