1zk5: Difference between revisions

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-[[Image:1zk5.png|left|200px]]
-{{STRUCTURE_1zk5|  PDB=1zk5  |  SCENE=  }}
+==Escherichia coli F17fG lectin domain complex with N-acetylglucosamine==
+<StructureSection load='1zk5' size='340' side='right'caption='[[1zk5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1zk5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZK5 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zk5 OCA], [https://pdbe.org/1zk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zk5 RCSB], [https://www.ebi.ac.uk/pdbsum/1zk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zk5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/F17FG_ECOLX F17FG_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 (By similarity).
+<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.
-===Escherichia coli F17fG lectin domain complex with N-acetylglucosamine===
+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>
-{{ABSTRACT_PUBMED_16041081}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1zk5" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[1zk5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZK5 OCA].
+*[[Adhesin 3D structures|Adhesin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:016041081</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Bouckaert, J.]]
+[[Category: Large Structures]]
-[[Category: Buts, L.]]
+[[Category: Bouckaert J]]
-[[Category: Genst, E De.]]
+[[Category: Buts L]]
-[[Category: Greve, H De.]]
+[[Category: De Genst E]]
-[[Category: Lahmann, M.]]
+[[Category: De Greve H]]
-[[Category: Loris, R.]]
+[[Category: Lahmann M]]
-[[Category: Molle, I Van.]]
+[[Category: Loris R]]
-[[Category: Oscarson, S.]]
+[[Category: Oscarson S]]
-[[Category: Wellens, A.]]
+[[Category: Van Molle I]]
-[[Category: Wyns, L.]]
+[[Category: Wellens A]]
-[[Category: Beta sandwich]]
+[[Category: Wyns L]]
-[[Category: Cell adhesion]]
-[[Category: Immunoglobulin-like fold]]
-[[Category: Lectin]]
-[[Category: Protein-structure complex]]