1zpl: Difference between revisions

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-[[Image:1zpl.png|left|200px]]
-<!--
+==E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me==
-The line below this paragraph, containing "STRUCTURE_1zpl", creates the "Structure Box" on the page.
+<StructureSection load='1zpl' size='340' side='right'caption='[[1zpl]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>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 [https://proteopedia.org/fgij/fg.htm?mol=1ZPL FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAG:BETA-METHYL-N-ACETYL-D-GLUCOSAMINE'>MAG</scene></td></tr>
-{{STRUCTURE_1zpl|  PDB=1zpl  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zpl OCA], [https://pdbe.org/1zpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zpl RCSB], [https://www.ebi.ac.uk/pdbsum/1zpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zpl ProSAT]</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.
-===E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me===
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1zpl" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16041081}}, adds the Publication Abstract to the page
+*[[Adhesin 3D structures|Adhesin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16041081 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16041081}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[1zpl]] is a 2 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=1ZPL OCA].
+[[Category: Bouckaert J]]
+[[Category: Buts L]]
-==Reference==
+[[Category: De Greve H]]
-<ref group="xtra">PMID:016041081</ref><references group="xtra"/>
+[[Category: Lahmann M]]
-[[Category: Escherichia coli]]
+[[Category: Loris R]]
-[[Category: Bouckaert, J.]]
+[[Category: Oscarson S]]
-[[Category: Buts, L.]]
+[[Category: Van Molle I]]
-[[Category: Greve, H De.]]
+[[Category: Wellens A]]
-[[Category: Lahmann, M.]]
+[[Category: Wyns L]]
-[[Category: Loris, R.]]
-[[Category: Molle, I Van.]]
-[[Category: Oscarson, S.]]
-[[Category: Wellens, A.]]
-[[Category: Wyns, L.]]
-[[Category: Bacterial adhesion]]
-[[Category: Cell adhesion]]
-[[Category: Fimbriae]]
-[[Category: Lectin]]
-[[Category: Protein-sugar complex]]