1zpl

<StructureSection load='1zpl' size='340' side='right' caption='[[1zpl]], [[Resolution|resolution]] 1.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[1zpl]] is a 2 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=1ZPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZPL FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAG:BETA-METHYL-N-ACETYL-D-GLUCOSAMINE'>MAG</scene></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=1zpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zpl OCA], [http://pdbe.org/1zpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zpl RCSB], [http://www.ebi.ac.uk/pdbsum/1zpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zpl ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/F17AG_ECOLX F17AG_ECOLX]] Essential fimbrial adhesion factor that mediates binding to N-acetylglucosamine-containing receptors in the host intestinal microvilli, leading to colonization of the intestinal tissue, and diarrhea or septicemia. Also confers adhesiveness to laminin and basement membranes.

<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.

 

== References ==

[[Category: Bacillus coli migula 1895]]

[[Category: Bouckaert, J]]

[[Category: Buts, L]]

[[Category: Greve, H De]]

[[Category: Lahmann, M]]

[[Category: Loris, R]]

[[Category: Molle, I Van]]

[[Category: Oscarson, S]]

[[Category: Wellens, A]]

[[Category: Wyns, L]]

[[Category: Protein-sugar complex]]