3bff

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="3bff" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bff, resolution 1.9&Aring;" /> '''class A beta-lactamas...)
Line 4: Line 4:
==Overview==
==Overview==
-
SED-1, a class A beta-lactamase from Citrobacter sedlakii, is a CTX-M-type, extended-spectrum beta-lactamase that has the ability to hydrolyze, expanded-spectrum cephalosporins such as cefotaxime. SED-1 and a SED, mutant in which Gly238 has been replaced by a cysteine, forming a, disulfide bridge with the other Cys residue located at position 69, (SED-G238C), have been crystallized. The crystals belong to the monoclinic, space group C2, with unit-cell parameters a = 188.09, b = 73.65, c =, 105.41 A, beta = 121.67 degrees for SED-1 and a = 187.64, b = 73.2, c =, 103.89 A, beta = 121.89 degrees for the SED-G238C mutant. X-ray, diffraction data were collected to maximum resolutions of 2.4 A for SED-1, and 2.0 A for SED-G238C.
+
SED-1, a class A beta-lactamase from Citrobacter sedlakii, is a CTX-M-type extended-spectrum beta-lactamase that has the ability to hydrolyze expanded-spectrum cephalosporins such as cefotaxime. SED-1 and a SED mutant in which Gly238 has been replaced by a cysteine, forming a disulfide bridge with the other Cys residue located at position 69 (SED-G238C), have been crystallized. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 188.09, b = 73.65, c = 105.41 A, beta = 121.67 degrees for SED-1 and a = 187.64, b = 73.2, c = 103.89 A, beta = 121.89 degrees for the SED-G238C mutant. X-ray diffraction data were collected to maximum resolutions of 2.4 A for SED-1 and 2.0 A for SED-G238C.
==About this Structure==
==About this Structure==
Line 26: Line 26:
[[Category: hydrolase]]
[[Category: hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:37:56 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:05:20 2008''

Revision as of 17:05, 21 February 2008

Image:3bff.jpg

3bff, resolution 1.9Å

Drag the structure with the mouse to rotate

class A beta-lactamase SED-G238C complexed with faropenem

Overview

SED-1, a class A beta-lactamase from Citrobacter sedlakii, is a CTX-M-type extended-spectrum beta-lactamase that has the ability to hydrolyze expanded-spectrum cephalosporins such as cefotaxime. SED-1 and a SED mutant in which Gly238 has been replaced by a cysteine, forming a disulfide bridge with the other Cys residue located at position 69 (SED-G238C), have been crystallized. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 188.09, b = 73.65, c = 105.41 A, beta = 121.67 degrees for SED-1 and a = 187.64, b = 73.2, c = 103.89 A, beta = 121.89 degrees for the SED-G238C mutant. X-ray diffraction data were collected to maximum resolutions of 2.4 A for SED-1 and 2.0 A for SED-G238C.

About this Structure

3BFF is a Single protein structure of sequence from Citrobacter sedlakii with , and as ligands. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.

Reference

Crystallization and preliminary X-ray diffraction study of the class A beta-lactamase SED-1 and its mutant SED-G238C from Citrobacter sedlakii., Petrella S, Pernot L, Sougakoff W, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):125-8. Epub 2003, Dec 18. PMID:14684905

Page seeded by OCA on Thu Feb 21 19:05:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bff"
Personal tools