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2kt4

From Proteopedia

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Current revision

Lipocalin Q83 is a Siderocalin

Structural highlights

2kt4 is a 1 chain structure with sequence from Cotja. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[EXFAB_COTJA] 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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Siderocalins are atypical lipocalins able to capture siderophores with high affinity. They contribute to the innate immune response by interfering with bacterial siderophore-mediated iron uptake but are also involved in numerous physiological processes such as inflammation, iron delivery, tissue differentiation, and cancer progression. The Q83 lipocalin was originally identified based on its overexpression in quail embryo fibroblasts transformed by the v-myc oncogene. We show here that Q83 is a siderocalin, binding the siderophore enterobactin with an affinity and mode of binding nearly identical to that of neutrophil gelatinase-associated lipocalin (NGAL), the prototypical siderocalin. This strengthens the role of siderocalins in cancer progression and inflammation. In addition, we also present the solution structure of Q83 in complex with intact enterobactin and a detailed analysis of the Q83 binding mode, including mutagenesis of the critical residues involved in enterobactin binding. These data provide a first insight into the molecular details of siderophore binding and delineate the common molecular properties defining the siderocalin protein family.

The v-myc-induced Q83 lipocalin is a siderocalin.,Coudevylle N, Geist L, Hotzinger M, Hartl M, Kontaxis G, Bister K, Konrat R J Biol Chem. 2010 Dec 31;285(53):41646-52. Epub 2010 Sep 8. PMID:20826777^[3]

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

References

↑ Coudevylle N, Geist L, Hotzinger M, Hartl M, Kontaxis G, Bister K, Konrat R. The v-myc-induced Q83 lipocalin is a siderocalin. J Biol Chem. 2010 Dec 31;285(53):41646-52. Epub 2010 Sep 8. PMID:20826777 doi:10.1074/jbc.M110.123331
↑ Coudevylle N, Hoetzinger M, Geist L, Kontaxis G, Hartl M, Bister K, Konrat R. Lipocalin Q83 reveals a dual ligand binding mode with potential implications for the functions of siderocalins. Biochemistry. 2011 Nov 1;50(43):9192-9. Epub 2011 Oct 7. PMID:21951132 doi:http://dx.doi.org/10.1021/bi201115q
↑ Coudevylle N, Geist L, Hotzinger M, Hartl M, Kontaxis G, Bister K, Konrat R. The v-myc-induced Q83 lipocalin is a siderocalin. J Biol Chem. 2010 Dec 31;285(53):41646-52. Epub 2010 Sep 8. PMID:20826777 doi:10.1074/jbc.M110.123331

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kt4"

@@ Line 1: / Line 1: @@
 ==Lipocalin Q83 is a Siderocalin==
-<StructureSection load='2kt4' size='340' side='right' caption='[[2kt4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2kt4' size='340' side='right'caption='[[2kt4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2kt4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cotja Cotja]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KT4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2kt4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cotja Cotja]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KT4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EB4:N,N,N-[(3S,7S,11S)-2,6,10-TRIOXO-1,5,9-TRIOXACYCLODODECANE-3,7,11-TRIYL]TRIS(2,3-DIHYDROXYBENZAMIDE)'>EB4</scene>, <scene name='pdbligand=GA:GALLIUM+(III)+ION'>GA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EB4:N,N,N-[(3S,7S,11S)-2,6,10-TRIOXO-1,5,9-TRIOXACYCLODODECANE-3,7,11-TRIYL]TRIS(2,3-DIHYDROXYBENZAMIDE)'>EB4</scene>, <scene name='pdbligand=GA:GALLIUM+(III)+ION'>GA</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=2kt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kt4 OCA], [http://pdbe.org/2kt4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kt4 RCSB], [http://www.ebi.ac.uk/pdbsum/2kt4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kt4 ProSAT]</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=2kt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kt4 OCA], [https://pdbe.org/2kt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kt4 RCSB], [https://www.ebi.ac.uk/pdbsum/2kt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kt4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/EXFAB_COTJA EXFAB_COTJA]] 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.<ref>PMID:20826777</ref> <ref>PMID:21951132</ref>
+[[https://www.uniprot.org/uniprot/EXFAB_COTJA EXFAB_COTJA]] 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.<ref>PMID:20826777</ref> <ref>PMID:21951132</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Cotja]]
+[[Category: Large Structures]]
 [[Category: Bister, K]]
 [[Category: Coudevylle, N]]

2kt4

From Proteopedia

Current revision

Lipocalin Q83 is a Siderocalin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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