1oi8: Difference between revisions

Revision as of 17:14, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1oi8.png

Template:STRUCTURE 1oi8

5'-NUCLEOTIDASE (E. COLI) WITH AN ENGINEERED DISULFIDE BRIDGE (P90C, L424C)5'-NUCLEOTIDASE (E. COLI) WITH AN ENGINEERED DISULFIDE BRIDGE (P90C, L424C)

Template:ABSTRACT PUBMED 15215524

About this StructureAbout this Structure

1OI8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges., Schultz-Heienbrok R, Maier T, Strater N, Protein Sci. 2004 Jul;13(7):1811-22. PMID:15215524

Page seeded by OCA on Sun Jul 27 17:14:20 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1oi8.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1oi8|  PDB=1oi8  |  SCENE=  }}
-'''5'-NUCLEOTIDASE (E. COLI) WITH AN ENGINEERED DISULFIDE BRIDGE (P90C, L424C)'''
+===5'-NUCLEOTIDASE (E. COLI) WITH AN ENGINEERED DISULFIDE BRIDGE (P90C, L424C)===
-==Overview==
+<!--
-Engineering disulfide bridges is a common technique to lock a protein movement in a defined conformational state. We have designed two double mutants of Escherichia coli 5'-nucleotidase to trap the enzyme in both an open (S228C, P513C) and a closed (P90C, L424C) conformation by the formation of disulfide bridges. The mutant proteins have been expressed, purified, and crystallized, to structurally characterize the designed variants. The S228C, P513C is a double mutant crystallized in two different crystal forms with three independent conformers, which differ from each other by a rotation of up to 12 degrees of the C-terminal domain with respect to the N-terminal domain. This finding, as well as an analysis of the domain motion in the crystal, indicates that the enzyme still exhibits considerable residual domain flexibility. In the double mutant that was designed to trap the enzyme in the closed conformation, the structure analysis reveals an unexpected intermediate conformation along the 96 degrees rotation trajectory between the open and closed enzyme forms. A comparison of the five independent conformers analyzed in this study shows that the domain movement of the variant enzymes is characterized by a sliding movement of the residues of the domain interface along the interface, which is in contrast to a classical closure motion where the residues of the domain interface move perpendicular to the interface.
+The line below this paragraph, {{ABSTRACT_PUBMED_15215524}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15215524 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15215524}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Metalloprotein]]
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