1zpl

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[[Image:1zpl.gif|left|200px]]<br /><applet load="1zpl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zpl.gif|left|200px]]
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caption="1zpl, resolution 1.7&Aring;" />
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'''E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me'''<br />
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{{Structure
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|PDB= 1zpl |SIZE=350|CAPTION= <scene name='initialview01'>1zpl</scene>, resolution 1.7&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MAG:ALPHA-METHYL-N-ACETYL-D-GLUCOSAMINE'>MAG</scene>
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|ACTIVITY=
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|GENE= F17G AF022140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZPL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MAG:'>MAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPL OCA].
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1ZPL 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].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16041081 16041081]
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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: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: bacterial adhesion]]
[[Category: bacterial adhesion]]
[[Category: fimbriae]]
[[Category: fimbriae]]
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[[Category: lectins]]
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[[Category: lectin]]
[[Category: protein-sugar complex]]
[[Category: protein-sugar complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:38:20 2008''

Revision as of 13:38, 20 March 2008


PDB ID 1zpl

Drag the structure with the mouse to rotate
, resolution 1.7Å
Ligands:
Gene: F17G AF022140 (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me


Overview

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.

About this Structure

1ZPL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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