2bsb: Difference between revisions
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==E. | |||
==E. coli F17e-G lectin domain complex with N-acetylglucosamine== | |||
<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 == | ||
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</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://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> | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bsb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2bsb" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2bsb" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Adhesin|Adhesin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:40, 16 May 2018
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. See AlsoReferences
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