2bs8: Difference between revisions
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==Crystal structure of F17b-G in complex with N-acetyl-D-glucosamine== | |||
<StructureSection load='2bs8' size='340' side='right' caption='[[2bs8]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bs8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BS8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bs7|2bs7]]</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=2bs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bs8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bs8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bs8 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Since the introduction of structural genomics, the protein has been recognized as the most important variable in crystallization. Recent strategies to modify a protein to improve crystal quality have included rationally engineered point mutations, truncations, deletions and fusions. Five naturally occurring variants, differing in 1-18 amino acids, of the 177-residue lectin domain of the F17G fimbrial adhesin were expressed and purified in identical ways. For four out of the five variants crystals were obtained, mostly in non-isomorphous space groups, with diffraction limits ranging between 2.4 and 1.1 A resolution. A comparative analysis of the crystal-packing contacts revealed that the variable amino acids are often involved in lattice contacts and a single amino-acid substitution can suffice to radically change crystal packing. A statistical approach proved reliable to estimate the compatibilities of the variant sequences with the observed crystal forms. In conclusion, natural variation, universally present within prokaryotic species, is a valuable genetic resource that can be favourably employed to enhance the crystallization success rate with considerably less effort than other strategies. | |||
Impact of natural variation in bacterial F17G adhesins on crystallization behaviour.,Buts L, Wellens A, Van Molle I, Wyns L, Loris R, Lahmann M, Oscarson S, De Greve H, Bouckaert J Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1149-59. Epub 2005, Jul 20. PMID:16041081<ref>PMID:16041081</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Bouckaert, J | [[Category: Bouckaert, J]] | ||
[[Category: Buts, L | [[Category: Buts, L]] | ||
[[Category: DeGreve, H | [[Category: DeGreve, H]] | ||
[[Category: Lahmann, M | [[Category: Lahmann, M]] | ||
[[Category: Loris, R | [[Category: Loris, R]] | ||
[[Category: Oscarson, S | [[Category: Oscarson, S]] | ||
[[Category: VanMolle, I | [[Category: VanMolle, I]] | ||
[[Category: Wellens, A | [[Category: Wellens, A]] | ||
[[Category: Wyns, L | [[Category: Wyns, L]] | ||
[[Category: Fimbriae]] | [[Category: Fimbriae]] | ||
[[Category: Lectin]] | [[Category: Lectin]] | ||
[[Category: Protein-sugar complex]] | [[Category: Protein-sugar complex]] | ||
[[Category: Sugar-binding protein]] | [[Category: Sugar-binding protein]] | ||