1bbp: Difference between revisions
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 3: | Line 3: | ||
<StructureSection load='1bbp' size='340' side='right'caption='[[1bbp]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1bbp' size='340' side='right'caption='[[1bbp]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bbp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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]] 2Å</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> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 14: | Line 15: | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bb/1bbp_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bb/1bbp_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 33: | Line 34: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pieris brassicae]] | ||
[[Category: Deutzmann | [[Category: Deutzmann R]] | ||
[[Category: Falk | [[Category: Falk H]] | ||
[[Category: Huber | [[Category: Huber R]] | ||
[[Category: Kayser | [[Category: Kayser H]] | ||
[[Category: Mayr | [[Category: Mayr I]] | ||
[[Category: Mueller | [[Category: Mueller R]] | ||
[[Category: Schneider | [[Category: Schneider M]] | ||
[[Category: Suter | [[Category: Suter F]] | ||
[[Category: Zuber | [[Category: Zuber H]] | ||
Latest revision as of 10:17, 23 October 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
FunctionBBP_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. Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||