1bsq

<StructureSection load='1bsq' size='340' side='right' caption='[[1bsq]], [[Resolution|resolution]] 2.22&Aring;' scene=''>

<table><tr><td colspan='2'>[[1bsq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BSQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BSQ FirstGlance]. <br>

</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=1bsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsq OCA], [http://pdbe.org/1bsq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bsq RCSB], [http://www.ebi.ac.uk/pdbsum/1bsq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bsq ProSAT]</span></td></tr>

[[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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/1bsq_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The structure of the trigonal crystal form of bovine beta-lactoglobulin variant B at pH 7.1 has been determined by X-ray diffraction methods at a resolution of 2.22 A and refined to values for R and Rfree of 0.239 and 0.286, respectively. By comparison with the structure of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 7.1, which was determined previously [Qin BY et al., 1998, Biochemistry 37:14014-14023], the structural consequences of the sequence differences D64G and V118A of variants A and B, respectively, have been investigated. Only minor differences in the core calyx structure occur. In the vicinity of the mutation site D64G on loop CD (residues 61-67), there are small changes in main-chain conformation, whereas the substitution V118A on beta-strand H is unaccompanied by changes in the surrounding structure, thereby creating a void volume and weakened hydrophobic interactions with a consequent loss of thermal stability relative to variant A. A conformational difference is found for the loop EF, implicated in the pH-dependent conformational change known as the Tanford transition, but it is not clear whether this reflects differences intrinsic to the variants in solution or differences in crystallization.

 

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== References ==

[[Category: Baker, E N]]

[[Category: Bewley, M C]]

[[Category: Creamer, L K]]

[[Category: Jameson, G B]]

[[Category: Qin, B Y]]

[[Category: Bovine beta-lactoglobulin]]

[[Category: Point mutation]]