We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1oid

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1oid.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1oid.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1oid| PDB=1oid | SCENE= }}
{{STRUCTURE_1oid| PDB=1oid | SCENE= }}
-
'''5'-NUCLEOTIDASE (E. COLI) WITH AN ENGINEERED DISULFIDE BRIDGE (S228C, P513C)'''
+
===5'-NUCLEOTIDASE (E. COLI) WITH AN ENGINEERED DISULFIDE BRIDGE (S228C, P513C)===
-
==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==
==About this Structure==
Line 30: Line 34:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Metalloprotein]]
[[Category: Metalloprotein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:53:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:39:54 2008''

Revision as of 06:39, 28 July 2008

Image:1oid.png

Template:STRUCTURE 1oid

5'-NUCLEOTIDASE (E. COLI) WITH AN ENGINEERED DISULFIDE BRIDGE (S228C, P513C)

Template:ABSTRACT PUBMED 15215524

About this Structure

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

Reference

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 Mon Jul 28 09:39:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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