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2uyw

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Current revision

Crystal structure of Xenavidin

Structural highlights

2uyw is a 2 chain structure with sequence from Xenopus tropicalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A7YYL1_XENTR

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

BACKGROUND: Avidins are proteins with extraordinarily high ligand-binding affinity, a property which is used in a wide array of life science applications. Even though useful for biotechnology and nanotechnology, the biological function of avidins is not fully understood. Here we structurally and functionally characterise a novel avidin named xenavidin, which is to our knowledge the first reported avidin from a frog. RESULTS: Xenavidin was identified from an EST sequence database for Xenopus tropicalis and produced in insect cells using a baculovirus expression system. The recombinant xenavidin was found to be homotetrameric based on gel filtration analysis. Biacore sensor analysis, fluorescently labelled biotin and radioactive biotin were used to evaluate the biotin-binding properties of xenavidin - it binds biotin with high affinity though less tightly than do chicken avidin and bacterial streptavidin. X-ray crystallography revealed structural conservation around the ligand-binding site, while some of the loop regions have a unique design. The location of structural water molecules at the entrance and/or within the ligand-binding site may have a role in determining the characteristic biotin-binding properties of xenavidin. CONCLUSION: The novel data reported here provide information about the biochemically and structurally important determinants of biotin binding. This information may facilitate the discovery of novel tools for biotechnology.

Structural and functional characteristics of xenavidin, the first frog avidin from Xenopus tropicalis.,Maatta JA, Helppolainen SH, Hytonen VP, Johnson MS, Kulomaa MS, Airenne TT, Nordlund HR BMC Struct Biol. 2009 Sep 29;9:63. PMID:19788720^[1]

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

References

↑ Maatta JA, Helppolainen SH, Hytonen VP, Johnson MS, Kulomaa MS, Airenne TT, Nordlund HR. Structural and functional characteristics of xenavidin, the first frog avidin from Xenopus tropicalis. BMC Struct Biol. 2009 Sep 29;9:63. PMID:19788720 doi:10.1186/1472-6807-9-63

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/2uyw"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF XENAVIDIN==
-<StructureSection load='2uyw' size='340' side='right' caption='[[2uyw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+==Crystal structure of Xenavidin==
+<StructureSection load='2uyw' size='340' side='right'caption='[[2uyw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2uyw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Silurana_(xenopus)_tropicalis Silurana (xenopus) tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UYW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2uyw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UYW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 1.7&#8491;</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=2uyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyw OCA], [http://pdbe.org/2uyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uyw RCSB], [http://www.ebi.ac.uk/pdbsum/2uyw PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></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=2uyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyw OCA], [https://pdbe.org/2uyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uyw RCSB], [https://www.ebi.ac.uk/pdbsum/2uyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uyw ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/A7YYL1_XENTR A7YYL1_XENTR]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uy/2uyw_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uy/2uyw_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 27: / Line 31: @@
 ==See Also==
-*[[Avidin|Avidin]]
+*[[Avidin 3D structures|Avidin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Airenne, T T]]
+[[Category: Large Structures]]
-[[Category: Helppolainen, S H]]
+[[Category: Xenopus tropicalis]]
-[[Category: Johnson, M S]]
+[[Category: Airenne TT]]
-[[Category: Kulomaa, M S]]
+[[Category: Helppolainen SH]]
-[[Category: Maatta, J A.E]]
+[[Category: Johnson MS]]
-[[Category: Nordlund, H R]]
+[[Category: Kulomaa MS]]
-[[Category: Avidin]]
+[[Category: Maatta JAE]]
-[[Category: Beta-barrel]]
+[[Category: Nordlund HR]]
-[[Category: Biotin-binding protein]]
-[[Category: Glycoprotein]]

2uyw

From Proteopedia

Current revision

Crystal structure of Xenavidin

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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