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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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AKQ FirstGlance]. <br> | + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=2akq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2akq OCA], [http://pdbe.org/2akq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2akq RCSB], [http://www.ebi.ac.uk/pdbsum/2akq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2akq 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=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 == |
| - | [[http://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. | + | [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]] |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Adams, J J]] | + | [[Category: Adams JJ]] |
| - | [[Category: Anderson, B F]] | + | [[Category: Anderson BF]] |
| - | [[Category: Creamer, L K]] | + | [[Category: Creamer LK]] |
| - | [[Category: Jameson, G B]] | + | [[Category: Jameson GB]] |
| - | [[Category: Norris, G E]] | + | [[Category: Norris GE]] |
| - | [[Category: B-lactoglbulin]]
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| - | [[Category: Crystal lattice]]
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| - | [[Category: Low ionic strength]]
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| - | [[Category: Pseudo-merohedral twinning]]
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| - | [[Category: Transport protein]]
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| 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 PubMed
Bovine 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 Also
References
- ↑ Adams JJ, Anderson BF, Norris GE, Creamer LK, Jameson GB. Structure of bovine beta-lactoglobulin (variant A) at very low ionic strength. J Struct Biol. 2006 Jun;154(3):246-54. Epub 2006 Feb 6. PMID:16540345 doi:10.1016/j.jsb.2005.12.010
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