1bbp: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 3: Line 3:
<StructureSection load='1bbp' size='340' side='right'caption='[[1bbp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1bbp' size='340' side='right'caption='[[1bbp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bbp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Large_white_butterfly Large white butterfly]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BBP FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bbp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pieris_brassicae Pieris brassicae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BBP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLV:BILIVERDIN+IX+GAMMA+CHROMOPHORE'>BLV</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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLV:BILIVERDIN+IX+GAMMA+CHROMOPHORE'>BLV</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=1bbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbp OCA], [https://pdbe.org/1bbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bbp RCSB], [https://www.ebi.ac.uk/pdbsum/1bbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bbp 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=1bbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbp OCA], [https://pdbe.org/1bbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bbp RCSB], [https://www.ebi.ac.uk/pdbsum/1bbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bbp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/BBP_PIEBR BBP_PIEBR]] This protein binds the blue pigments bilins.<ref>PMID:3202956</ref>
[https://www.uniprot.org/uniprot/BBP_PIEBR BBP_PIEBR] This protein binds the blue pigments bilins.<ref>PMID:3202956</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bbp ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bbp ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The bilin binding protein (BBP) from the insect Pieris brassicae has been analysed for amino acid sequence, spectral properties and three-dimensional structure. The crystal structure that had been determined by isomorphous replacement has been refined at 2.0 A (1 A = 0.1 nm) resolution to an R-value of 0.20. The asymmetric unit contains four independent subunits of BBP. The co-ordinate differences are 0.25 A, in accord with the estimated error in co-ordinates. The polypeptide chain fold is characterized by an eight-stranded barrel. The connecting loops splay out at the upper end of the barrel and open it, whilst the lower end is closed. The overall shape resembles a calyx. The biliverdin IX gamma chromophore is located in a central cleft at the upper end of the barrel. The bilatriene moiety is in cyclic helical geometry with configuration Z,Z,Z and conformation syn,syn,syn. The geometry is in accord with the spectral properties and permits a correlation between sign of the circular dichroism bands and sense of the bilatriene helices. The fold of BBP is related to retinol binding protein (RBP), as had been recognized in the preliminary analysis, although the amino acid sequences of RBP and BBP show only 10% homology. There are large differences in the loops at the upper end of the barrel, whilst the segments of the centre and the lower end of the barrel superimpose closely. The ligands of BBP and RBP, biliverdin and retinol, respectively, are also similarly located.
Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 A resolution.,Huber R, Schneider M, Mayr I, Muller R, Deutzmann R, Suter F, Zuber H, Falk H, Kayser H J Mol Biol. 1987 Dec 5;198(3):499-513. PMID:3430616<ref>PMID:3430616</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bbp" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
Line 33: Line 25:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Large white butterfly]]
[[Category: Pieris brassicae]]
[[Category: Deutzmann, R]]
[[Category: Deutzmann R]]
[[Category: Falk, H]]
[[Category: Falk H]]
[[Category: Huber, R]]
[[Category: Huber R]]
[[Category: Kayser, H]]
[[Category: Kayser H]]
[[Category: Mayr, I]]
[[Category: Mayr I]]
[[Category: Mueller, R]]
[[Category: Mueller R]]
[[Category: Schneider, M]]
[[Category: Schneider M]]
[[Category: Suter, F]]
[[Category: Suter F]]
[[Category: Zuber, H]]
[[Category: Zuber H]]
[[Category: Bilin binding]]

Revision as of 18:31, 13 March 2024

MOLECULAR STRUCTURE OF THE BILIN BINDING PROTEIN (BBP) FROM PIERIS BRASSICAE AFTER REFINEMENT AT 2.0 ANGSTROMS RESOLUTION.MOLECULAR STRUCTURE OF THE BILIN BINDING PROTEIN (BBP) FROM PIERIS BRASSICAE AFTER REFINEMENT AT 2.0 ANGSTROMS RESOLUTION.

Structural highlights

1bbp is a 4 chain structure with sequence from Pieris brassicae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BBP_PIEBR This protein binds the blue pigments bilins.[1]

Evolutionary Conservation

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

References

  1. ↑ Suter F, Kayser H, Zuber H. The complete amino-acid sequence of the bilin-binding protein from Pieris brassicae and its similarity to a family of serum transport proteins like the retinol-binding proteins. Biol Chem Hoppe Seyler. 1988 Jun;369(6):497-505. PMID:3202956

1bbp, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1bbp&oldid=4093907"