1zpl: Difference between revisions

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-{{Seed}}
-[[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]]
-ZPL is a [[Single protein]] structure of 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]]
-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:[http://www.ncbi.nlm.nih.gov/pubmed/16041081 16041081]
+[[Category: Lahmann M]]
-[[Category: Escherichia coli]]
+[[Category: Loris R]]
-[[Category: Single protein]]
+[[Category: Oscarson S]]
-[[Category: Bouckaert, J.]]
+[[Category: Van Molle I]]
-[[Category: Buts, L.]]
+[[Category: Wellens A]]
-[[Category: Greve, H De.]]
+[[Category: Wyns L]]
-[[Category: Lahmann, M.]]
-[[Category: Loris, R.]]
-[[Category: Molle, I Van.]]
-[[Category: Oscarson, S.]]
-[[Category: Wellens, A.]]
-[[Category: Wyns, L.]]
-[[Category: Bacterial adhesion]]
-[[Category: Fimbriae]]
-[[Category: Lectin]]
-[[Category: Protein-sugar complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:53:25 2008''