2akq: Difference between revisions
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<StructureSection load='2akq' size='340' side='right'caption='[[2akq]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='2akq' size='340' side='right'caption='[[2akq]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2akq]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2akq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mfh 1mfh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AKQ FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1beb|1beb]], [[1bso|1bso]], [[3blg|3blg]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1beb|1beb]], [[1bso|1bso]], [[3blg|3blg]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2akq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2akq OCA], [https://pdbe.org/2akq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2akq RCSB], [https://www.ebi.ac.uk/pdbsum/2akq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2akq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN]] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 17:42, 17 November 2021
The structure of bovine B-lactoglobulin A in crystals grown at very low ionic strengthThe structure of bovine B-lactoglobulin A in crystals grown at very low ionic strength
Structural highlights
Function[LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. 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 PubMedBovine beta-lactoglobulin (BLG) is a globular protein of uncertain physiological function and a member of the lipocalin superfamily of proteins. Here, we present the X-ray structure at 3.0 angstroms of BLG (variant A) from an orthorhombic (P2(1)2(1)2(1)) pseudo-tetragonal crystal form that suffers from pseudo-merohedral twinning (final R(working) = 0.224, R(free) = 0.265). Crystals were grown by dialysis against ultra-purified water (i.e., at very low ionic strength), at pH approximately 5.2 (approximately pI), conditions vastly different from all other BLG structures determined previously. This allows critical assessment of the BLG structure and of the influence that pH, ionic strength, and crystal packing may have on the molecular structure of BLG. The pH-sensitive EF loop is found in the closed conformation characteristic of BLG at pH less than 7 and moderate to high ionic strength. Although the hydrophobic pocket appears to be empty, the presence of highly disordered water molecules cannot be excluded. The dimer interface and the hydrophobic pocket (calyx) are preserved. However, the orientation of the subunits in the dimer varies considerably with crystal form. Structure is deposited with PDB ID 2akq. Structure of bovine beta-lactoglobulin (variant A) at very low ionic strength.,Adams JJ, Anderson BF, Norris GE, Creamer LK, Jameson GB J Struct Biol. 2006 Jun;154(3):246-54. Epub 2006 Feb 6. PMID:16540345[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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