3sao

From Proteopedia

(Difference between revisions)

Current revision

The Siderocalin Ex-FABP functions through dual ligand specificities

Structural highlights

3sao is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EXFAB_CHICK Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor.

Publication Abstract from PubMed

Galline Ex-FABP was identified as another candidate antibacterial, catecholate siderophore binding lipocalin (siderocalin) based on structural parallels with the family archetype, mammalian Siderocalin. Binding assays show that Ex-FABP retains iron in a siderophore-dependent manner in both hypertrophic and dedifferentiated chondrocytes, where Ex-FABP expression is induced after treatment with proinflammatory agents, and specifically binds ferric complexes of enterobactin, parabactin, bacillibactin and, unexpectedly, monoglucosylated enterobactin, which does not bind to Siderocalin. Growth arrest assays functionally confirm the bacteriostatic effect of Ex-FABP in vitro under iron-limiting conditions. The 1.8 A crystal structure of Ex-FABP explains the expanded specificity, but also surprisingly reveals an extended, multi-chambered cavity extending through the protein and encompassing two separate ligand specificities, one for bacterial siderophores (as in Siderocalin) at one end and one specifically binding copurified lysophosphatidic acid, a potent cell signaling molecule, at the other end, suggesting Ex-FABP employs dual functionalities to explain its diverse endogenous activities.

Galline Ex-FABP Is an Antibacterial Siderocalin and a Lysophosphatidic Acid Sensor Functioning through Dual Ligand Specificities.,Correnti C, Clifton MC, Abergel RJ, Allred B, Hoette TM, Ruiz M, Cancedda R, Raymond KN, Descalzi F, Strong RK Structure. 2011 Dec 7;19(12):1796-806. PMID:22153502^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Correnti C, Clifton MC, Abergel RJ, Allred B, Hoette TM, Ruiz M, Cancedda R, Raymond KN, Descalzi F, Strong RK. Galline Ex-FABP Is an Antibacterial Siderocalin and a Lysophosphatidic Acid Sensor Functioning through Dual Ligand Specificities. Structure. 2011 Dec 7;19(12):1796-806. PMID:22153502 doi:10.1016/j.str.2011.09.019

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3sao"

Categories: Gallus gallus | Large Structures | Clifton MC | Correnti C | Strong RK

@@ Line 1: / Line 1: @@
 ==The Siderocalin Ex-FABP functions through dual ligand specificities==
-<StructureSection load='3sao' size='340' side='right' caption='[[3sao]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='3sao' size='340' side='right'caption='[[3sao]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3sao]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SAO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3sao]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SAO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DBH:2,3-DIHYDROXY-BENZOIC+ACID'>DBH</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NKN:(2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL+TETRADECANOATE'>NKN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXFABP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DBH:2,3-DIHYDROXY-BENZOIC+ACID'>DBH</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NKN:(2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL+TETRADECANOATE'>NKN</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sao OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sao RCSB], [http://www.ebi.ac.uk/pdbsum/3sao PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sao OCA], [https://pdbe.org/3sao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sao RCSB], [https://www.ebi.ac.uk/pdbsum/3sao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sao ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/EXFAB_CHICK EXFAB_CHICK] Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 15: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3sao" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Fatty acid-binding protein|Fatty acid-binding protein]]
+*[[Siderocalin 3D structures|Siderocalin 3D structures]]
 == References ==
 <references/>
@@ Line 23: / Line 27: @@
 </StructureSection>
 [[Category: Gallus gallus]]
-[[Category: Clifton, M C]]
+[[Category: Large Structures]]
-[[Category: Correnti, C]]
+[[Category: Clifton MC]]
-[[Category: Strong, R K]]
+[[Category: Correnti C]]
-[[Category: Beta-barrel]]
+[[Category: Strong RK]]
-[[Category: Siderophore binding protein]]
-[[Category: Transport protein]]

3sao

From Proteopedia

Current revision

The Siderocalin Ex-FABP functions through dual ligand specificities

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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