1qff: Difference between revisions

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[[Image:1qff.jpg|left|200px]]<br /><applet load="1qff" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1qff.jpg|left|200px]]
caption="1qff, resolution 2.70&Aring;" />
 
'''E. COLI FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) IN COMPLEX WITH BOUND FERRICHROME-IRON'''<br />
{{Structure
|PDB= 1qff |SIZE=350|CAPTION= <scene name='initialview01'>1qff</scene>, resolution 2.70&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=FTT:3-HYDROXY-TETRADECANOIC+ACID'>FTT</scene>, <scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=EAP:2-AMINO-VINYL-PHOSPHATE'>EAP</scene>, <scene name='pdbligand=FCI:FERRICROCIN-IRON'>FCI</scene> and <scene name='pdbligand=DDQ:DECYLAMINE-N,N-DIMETHYL-N-OXIDE'>DDQ</scene>
|ACTIVITY=
|GENE=
}}
 
'''E. COLI FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) IN COMPLEX WITH BOUND FERRICHROME-IRON'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1QFF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=FTT:'>FTT</scene>, <scene name='pdbligand=DAO:'>DAO</scene>, <scene name='pdbligand=MYR:'>MYR</scene>, <scene name='pdbligand=DPO:'>DPO</scene>, <scene name='pdbligand=EAP:'>EAP</scene>, <scene name='pdbligand=FCI:'>FCI</scene> and <scene name='pdbligand=DDQ:'>DDQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFF OCA].  
1QFF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFF OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10873859 10873859]
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:[http://www.ncbi.nlm.nih.gov/pubmed/10873859 10873859]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 33: Line 42:
[[Category: tonb-dependent receptor]]
[[Category: tonb-dependent receptor]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:53 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:41 2008''

Revision as of 14:36, 20 March 2008

File:1qff.jpg


PDB ID 1qff

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands: , , , , , , and
Coordinates: save as pdb, mmCIF, xml



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

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