From Proteopedia
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- | [[Image:1zk5.gif|left|200px]] | + | {{Seed}} |
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| {{STRUCTURE_1zk5| PDB=1zk5 | SCENE= }} | | {{STRUCTURE_1zk5| PDB=1zk5 | SCENE= }} |
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- | '''Escherichia coli F17fG lectin domain complex with N-acetylglucosamine'''
| + | ===Escherichia coli F17fG lectin domain complex with N-acetylglucosamine=== |
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- | ==Overview==
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- | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16041081}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 16041081 is the PubMed ID number. |
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| + | {{ABSTRACT_PUBMED_16041081}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lectin]] | | [[Category: Lectin]] |
| [[Category: Protein-structure complex]] | | [[Category: Protein-structure complex]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:43:22 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:59:48 2008'' |
Revision as of 06:59, 28 July 2008
Template:STRUCTURE 1zk5
Escherichia coli F17fG lectin domain complex with N-acetylglucosamine
Template:ABSTRACT PUBMED 16041081
About this Structure
1ZK5 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
Page seeded by OCA on Mon Jul 28 09:59:48 2008
Categories: Escherichia coli | Single protein | Bouckaert, J. | Buts, L. | Genst, E De. | Greve, H De. | Lahmann, M. | Loris, R. | Molle, I Van. | Oscarson, S. | Wellens, A. | Wyns, L. | Beta sandwich | Immunoglobulin-like fold | Lectin | Protein-structure complex