This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1zpl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zpl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zpl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zpl| PDB=1zpl | SCENE= }}
{{STRUCTURE_1zpl| PDB=1zpl | SCENE= }}
-
'''E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me'''
+
===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.
+
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.
 +
-->
 +
{{ABSTRACT_PUBMED_16041081}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Lectin]]
[[Category: Lectin]]
[[Category: Protein-sugar complex]]
[[Category: Protein-sugar complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:55:05 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:53:25 2008''

Revision as of 12:53, 27 July 2008

Image:1zpl.png

Template:STRUCTURE 1zpl

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

Template:ABSTRACT PUBMED 16041081

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

Page seeded by OCA on Sun Jul 27 15:53:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zpl"
Personal tools