2bsb: Difference between revisions
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<StructureSection load='2bsb' size='340' side='right' caption='[[2bsb]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2bsb' size='340' side='right' caption='[[2bsb]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bsb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2bsb]] 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=2BSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BSB 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> | </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">[[2bsc|2bsc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bsc|2bsc]]</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=2bsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bsb RCSB], [http://www.ebi.ac.uk/pdbsum/2bsb PDBsum]</span></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=2bsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsb OCA], [http://pdbe.org/2bsb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bsb RCSB], [http://www.ebi.ac.uk/pdbsum/2bsb PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2bsb" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Bouckaert, J]] | [[Category: Bouckaert, J]] | ||
[[Category: Buts, L]] | [[Category: Buts, L]] | ||
Revision as of 17:22, 10 September 2015
E. COLI F17E-G LECTIN DOMAIN COMPLEX WITH N-ACETYLGLUCOSAMINEE. COLI F17E-G LECTIN DOMAIN COMPLEX WITH N-ACETYLGLUCOSAMINE
Structural highlights
Publication Abstract from PubMedSince 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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